DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Status of the Application
Receipt of the Request for Continued Examination (RCE under 37 CFR 1.114) and the Response and Amendment filed 2 February 2026 is acknowledged.
The status of the claims upon entry of the present amendment stands as follows:
Pending claims: 1-4, 9, 14, 17-20, 22, 24, 29, 33-35, 37, and 41-43
Withdrawn claims: None
Previously canceled claims: 5-8, 10-13, 15-16, 21, 23, 25-28, 30-32, 36, and 38-40
Newly canceled claims: None
Amended claims: 1
New claims: None
Claims currently under consideration: 1-4, 9, 14, 17-20, 22, 24, 29, 33-35, 37, and 41-43
Currently rejected claims: 1-4, 9, 14, 17-20, 22, 24, 29, 33-35, 37, and 41-43
Allowed claims: None
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 2 February 2026 has been entered.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
Claim 2 is rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
Regarding claim 2, a broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) may be considered indefinite if the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In the present instance, claim 2 recites the broad recitation “wherein the first retentate obtained in step (ii) prior to step (iii), the second retentate obtained in step (iii), or any other aqueous stream comprising potato proteins and optionally insoluble fibers obtained downstream of step (iii)”, and the claim also recites “preferably the second retentate obtained in step (iii)”, which is the narrower statement of the range/limitation. The claim is considered indefinite because there is a question or doubt as to whether the feature introduced by such narrower language is (a) merely exemplary of the remainder of the claim, and therefore not required, or (b) a required feature of the claims.
For purposes of examination, the limitation is considered to be, “The method according to claim 1, wherein the first retentate obtained in step (ii) prior to step (iii), the second retentate obtained in step (iii), or any other aqueous stream comprising potato proteins and optionally insoluble fibers obtained downstream of step (iii) is exposed to: a pH value between 2.0 and 4.5; a temperature in the range of 1-70 °C; and in a time span of up to 240 minutes.”
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1-4, 9, 14, 17-20, 24, 29, 33, 35, and 41-43 are rejected under 35 U.S.C. 103 as being unpatentable over Habeych Narvaez et al. (hereinafter “Habeych”) (US 2022/0240538 A1).
Regarding claim 1, Habeych teaches a method for separation of (a) potato proteins, comprising patatin and protease inhibitor, from (b) first salts and phenolic and/or glycoalkaloid compounds in potato fruit juice or a derivative thereof, said method comprising the steps of:
(i) providing a potato fruit juice or a derivative thereof, comprising:
potato proteins – tuber processing water, for example potato fruit juice as obtained after starch isolation ([0067]), was used as raw material for production of a total native (potato) protein isolate ([0137]). A total isolate comprises protease inhibitor and patatin ([0031]); and
one or more first salts – salts present in the tuber processing water (i.e., first salts) are replaced by diafiltration ([0035]); and
phenolic and/or glycoalkaloid compounds – the method also comprises a step of glycoalkaloid removal ([0091]) indicating the presence of glycoalkaloids in the potato fruit juice;
(ii) subjecting said potato fruit juice or the derivative thereof to a first cross-flow membrane filtration process wherein water and at least a portion of the first salts and at least a portion of the phenolic and/or glycoalkaloid compounds migrate across the membrane into a first permeate and wherein the potato proteins are retained in a first retentate – “The potato processing water was ultrafiltrated using a spiral-wound membrane with a molecular weight cut-off (MWCO) of 5 kDa…” ([0143]). The diafiltration membrane may have a MWCO of 3-500 kDa ([0036]). Regarding the passage of the first salts and phenolic and/or glycoalkaloid compounds across the membrane, at least a portion of these ions and small molecules would pass through the disclosed 5 kDa molecular-weight cut-off filter;
(iii) adding aqueous diafiltration liquid containing one or more salts to the first retentate obtained in step (ii) to form a diluted first retentate having a conductivity of between 1 mS/cm and 50 mS/cm and subjecting said diluted first retentate to a second cross-flow membrane filtration as diafiltration, to create a second permeate being a diafiltrate containing at least a portion of said phenolic and/or glycoalkaloid compounds and salts and a second retentate comprising potato proteins, and salts – “The retentate from the ultrafiltration [i.e., first retentate] was subjected to further treatment comprising diafiltration against a salt solution having 0.33 or 50.66 [sic, 0.66] wt. % NaCl [i.e., one or more salts]…This resulted in a potato protein isolate solution [i.e., second retentate].” ([0144]). “Each diafiltration step entails dilution of protein solution volume VPJ with diafiltration volume VDF in a ratio as indicated and concentrating the diluted protein solution back to the original volume by ultrafiltration.” ([0152]). “[I]t is essential that during the whole isolation process, the conductivity is relatively high. The salt solution against which the diafiltration is performed must have a conductivity of at least 5 mS/cm, and the feed solution must have a conductivity of 2-20 mS/cm.” ([0040]). “Preferably, the conductivity of the solution to be diafiltered (the diafiltration feed solution or feed) remains within the ranges herein specified.” ([0054]). Habeych further discloses that when the salt concentration was increased from 0.33% to 0.66%, the TGA (i.e., glycoalkaloid) content of the dried protein isolate was lower ([0148] and [0146], Table 2, Experiment 6, “Total TGA content”), indicating that at least a portion of glycoalkaloids pass through the filter during the diafiltration process. The resulting diafiltrate would also comprise salts since these ions would pass through the disclosed 5 kDa molecular-weight cut-off filter.
wherein the pH of the first retentate and the second retentate remains within the range of 4.5 to 8.5 during step (ii) and step (iii) – The pH of the diafiltration feed solution (e.g., from step (ii)) is preferably 5.5-7.0 ([0044]). “Preferably in this embodiment, the pH remains the same throughout all diafiltration stages.” (0054]). “In further preferred embodiments, the salt solution may have a pH of…5.5-8.0…In preferred embodiments, this pH is maintained throughout the diafiltration.” ([0050]). Since the pH of both the diafiltration feed solution and the salt solution are within the claimed range throughout the diafiltration process, the pH of the first and second retentates would also be within the claimed range.
said method further comprising a step of eliminating or reducing enzymatic activity by exposing:
the first retentate obtained in step (ii) prior to step (iii)
to pH values between 2.0 and 4.5 in a time and temperature interval sufficient to eliminate or reduce unwanted enzymatic activity of the potato proteins without adversely affecting functionality of the potato proteins, whereafter the pH is increased again to a value between 4.5 and 8.5 – Habeych teaches that the tuber processing water (i.e., potato fruit juice) is subjected to a pretreatment prior to the diafiltration step (i.e., prior to step (iii)) ([0020]). Pretreatment can comprise at least one of concentration, pH adjustment, solids removal, and/or heat treatment, resulting in a pretreated tuber processing water comprising native protein, and these steps can be performed in any order ([0070]). Concentration is preferably achieved through cross-flow ultrafiltration (i.e., as the claimed step (ii)) ([0074]). Paragraph [0082] reads:
[A] pH adjustment to 4.0-5.5 can be used to precipitate at least part of the patatin fraction…so as to obtain tuber processing water comprising a higher relative quantity of native protease inhibitor. Precipitated protein can subsequently be removed during a step of solids removal as elsewhere defined. This increases the relative quantity of native protease inhibitor in the native tuber protein isolate.
Paragraph [0084] reads:
A heat treatment may also be applied as a pretreatment, provided that the heat treatment does not result in full protein coagulation. For example, a heat treatment to 40-55° C. for 1-120 minutes may remove a significant portion of the patatin, which can subsequently be removed by a solids removal step. Also, it is known that protease inhibitor from tuber has higher heat stability than patatin, and that heating may lead to partial or full denaturation of patatin. Thus, a heating step may be performed in combination with a solids removal step for example to obtain a tuber processing water enriched in native protease inhibitor. For example, a heat treatment at 60-80° C., preferably 70-73° C. can be used to precipitate at least part of the patatin fraction, which can be followed by a step of solids removal, in order to isolate native tuber protein enriched in native protease inhibitor.
The claimed pH range of between 2.0 and 4.5 overlaps with the disclosed pH range of 4.0-5.5. In a case where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists, MPEP § 2144.05(I).
Habeych discloses precipitating and removing at least part of the patatin to enrich the amount of protease inhibitor. This does not require precipitating and removing all of the patatin. Habeych teaches that the pH of the diafiltration feed solution (e.g., from step (ii)) is preferably 5.5-7.0 ([0044]). “Preferably in this embodiment, the pH remains the same throughout all diafiltration stages.” (0054]). As such, one of ordinary skill in the art would have found it obvious to increase the pH to a value of 5.5 to 7.0 (i.e., between 4.5 and 8.5 as claimed) after this pretreatment, and before diafiltration. Therefore, the remaining patatin, along with the protease inhibitors and other potato proteins, would be treated as claimed. Furthermore, one of ordinary skill in the art of potato protein purification would have had an understanding of the biochemical properties of the potato proteins and would have used process parameters within the disclosed ranges to obtain desired functional properties of said proteins.
or said method further comprising a step of eliminating or reducing enzymatic activity by exposing:
the second retentate obtained in step (iii); or
any other aqueous stream comprising potato proteins and optionally insoluble fibers obtained downstream of step (iii),
to pH values between 2.0 and 4.5 in a time and temperature interval sufficient to eliminate or reduce unwanted enzymatic activity of the potato proteins without adversely affecting functionality of the potato proteins, whereafter the pH is increased again to a value between 4.5 and 8.5 – Habeych teaches that the protein isolate is dried by various methods, such as spray drying ([0060], see also [0148]). Habeych teaches that it is preferred to adjust the pH of a concentrated aqueous tuber protein isolate, particularly those comprising tuber protease inhibitor, to higher than 2.5 to stabilize the viscosity of the protein solution and avoid gelling of the solution during storage prior to drying ([0063]). Habeych also teaches that it is preferred to adjust the pH of a concentrated tuber protein isolate, particularly those comprising tuber patatin, to lower than 4.0, also in order to stabilize the viscosity of the protein solution during storage prior to drying ([0064]). Therefore, Habeych teaches that it is preferred to adjust the pH of concentrated aqueous tuber protein isolates comprising protease inhibitors and patatin to a pH between 2.5 and 4.0 to stabilize the viscosity of the protein solution during storage prior to drying.
Habeych further teaches, “It is much preferred hat prior to drying, the tuber protein isolate is adjusted to a pH of 5.5-7.0…This increases the stability of the native tuber protein powder, which facilitates storage.” ([0062]). Additionally, Habeych teaches, “In much preferred embodiments, the method is performed so as to keep the temperature of the tuber processing water below 40° C. during the pretreatment, the diafiltration and any other step prior to drying.” ([0103]).
Therefore, given these teachings, it would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, after diafiltration to reduce the pH of the concentrated aqueous tuber protein isolate to a value between 2.5 and 4.0 and a temperature below 40 °C to stabilize the viscosity of the protein solution during storage prior to drying, and subsequently increase the pH to a value between 5.5 and 7.0 just before drying to increase the stability of the protein powder.
While Habeych does not discuss that such treatment eliminates or reduces enzymatic activity of the potato proteins without adversely affecting functionality of the potato proteins, Habeych nonetheless discloses the claimed steps. When the method steps recited in the prior art reference are substantially identical to those of the claims, claimed properties of the resulting composition are presumed to be present in the composition of the prior art. The burden of proof shifts to the applicant to provide objective evidence (i.e., test data) to the contrary. See In re Best, 562, F.2d 1252, 1254, 195 USPQ 403, 433 (CCPA 1977). MPEP § 2112.01(I).
Indeed, pages 44-45 and Figure 7 of the instant application demonstrate that treatment of the diafiltration retentate with a pH of 3.0 or 4.0 at room temperature or 40 °C for at least 15 minutes reduces esterase activity of the proteins and that functionality is retained after increasing the pH. Where Habeych teaches conducting the steps as claimed, the properties of eliminating or reducing enzyme activity of the potato proteins without adversely affecting functionality of the potato proteins are presumed to be present.
Therefore, claim 1 is rendered obvious.
Regarding claim 2, Habeych teaches the method according to claim 1.
Habeych also teaches that the first retentate obtained in step (ii) prior to step (iii) is exposed to:
a pH value between 2.0 and 4.5 – 4.0-5.5 ([0082]);
a temperature in the range of 1-70 °C – 40-55 °C ([0084]); and
in a time span of up to 240 minutes – 1-120 minutes ([0084]).
As described regarding claim 1 above, Habeych also teaches that the second retentate obtained in step (iii) or any other aqueous stream comprising potato proteins and optionally insoluble fibers obtained downstream of step (iii) is exposed to:
a pH value between 2.0 and 4.5 – 2.5-4.0 ([0062] – [0063]);
a temperature in the range of 1-70 °C – below 40 °C ([0103]). The claimed range overlaps the disclosed range. In a case where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists, MPEP § 2144.05(I).
in a time span of up to 240 minutes – “during storage prior to drying” ([0062] – [0063]). It is considered that one of ordinray skill in the art would have dried the native protein solution within 240 minutes (4 hours) during a day’s work. It is well-known in protein biochemistry that purified proteins in solution lose stability over time. Therfore, one of ordinary skill in the art would have been motivated to dry the purified proteins as soon as is feasible. Absent any evidence of criticality, the claimed timeframe is obvious.
Therefore, claim 2 is rendered obvious.
Regarding claim 3, Habeych teaches the method according to claim 1.
Habeych also teaches that the first cross-flow membrane filtration process is an ultrafiltration process – “In all cases, the pretreatment furthermore comprised an ultrafiltration step preceding the diafiltration.” ([0143]). “In preferred embodiments, the ultrafiltration is performed as a continuous (cross-flow) process ([0074]).” Therefore, claim 3 is rendered obvious.
Regarding claim 4, Habeych teaches the method according to claim 1.
Habeych also teaches that the second cross-flow membrane filtration process is an ultrafiltration process – “In all cases, the pretreatment furthermore comprised an ultrafiltration step preceding the diafiltration.” ([0143]). “In preferred embodiments, the ultrafiltration is performed as a continuous (cross-flow) process.” ([0074]). “In preferred embodiments, an ultrafiltration pretreatment is performed using the same setup as the diafiltration step.” ([0078]). The use of the same setup indicates that the claimed second membrane filtration process (diafiltration) is also a cross-flow ultrafiltration process. Therefore, claim 4 is rendered obvious.
Regarding claim 9, Habeych teaches the method according to claim 1.
Habeych also teaches that the method further comprises the step of subjecting the second retentate to the claimed “fifth” membrane filtration process resulting in a “fifth” retentate, wherein at least a portion of the salts migrate across the membrane into a “fifth” permeate – Analogous to the workflow of instant Figure 4, Habeych teaches that after a diafiltration with a salt solution, the retentate (i.e., second retentate) is subjected to salts removal via “a diafiltration stage against water at lower conductivity, or against regular water, in order to remove salts and isolate native tuber protein essentially free of salt” ([0053]). As such, salts migrate across the membrane into a “fifth” permeate. Therefore, claim 9 is rendered obvious.
Regarding claim 14, Habeych teaches the method according to claim 1.
Habeych also teaches that the aqueous diafiltration liquid containing one or more salts contains one or more second salts that are added to the aqueous diafiltration liquid and that are different from the one or more first salts – Habeych discloses sulfite added to tuber processing water during starch processing, which is removed by the method ([0112]). The disclosed sulfite is seen as the first salt. Habeych also teaches that the diafiltration is performed against a salt solution ([0045]) preferably comprising a chloride salt, such as sodium chloride, potassium chloride, or calcium chloride ([0046]). The disclosed chloride salts are seen as second salts that are different than the first salt. Therefore, claim 14 is rendered obvious.
Regarding claim 17, Habeych teaches the method according to claim 1.
Habeych also teaches that the method further comprises the step of adjusting the pH of said potato fruit juice or the derivative thereof to a pH in the range of 4.5 to 8.5 prior to said first cross-flow membrane filtration process – “The pretreatment may include one or more pH adjustments.” ([0080]). “For example, a pH adjustment to 4.0-5.5 can be used to precipitate at least part of the patatin fraction…” ([0082]). The claimed range overlaps the disclosed range. In a case where the claimed ranges overlap or lie inside ranges disclosed by the prior art, a prima facie case of obviousness exists, MPEP § 2144.05(I). Therefore, claim 17 is rendered obvious.
Regarding claim 18, Habeych teaches the method according to claim 1.
Habeych also teaches that the method further comprises the step of adjusting the conductivity of said potato fruit juice or the derivative thereof to a conductivity in the range of 2-500 mS/cm prior to said first cross-flow membrane filtration process – “pretreatment results in a pretreated tuber processing water having a conductivity of 2-20 mS/cm…” ([0020]). The disclosed range lies within the claimed range. Therefore, claim 18 is rendered obvious.
Regarding claim 19, Habeych teaches the method according to claim 1.
Habeych also teaches that the potato proteins are selected from the group consisting of patatin and protease inhibitors – “the tuber protein isolate is isolate comprising native protease inhibitor and native patatin. In further much preferred embodiments, the tuber protein isolate is a total native tuber protein isolate.” ([0030]). Therefore claim 19 is rendered obvious.
Regarding claim 20, Habeych teaches the method according to claim 1.
Habeych also teaches that the potato fruit juice or the derivative thereof is pretreated by centrifugation and/or filtration to remove insoluble material of a particle size larger than 10 microns prior to said first cross-flow membrane filtration process – Habeych discloses solids removal as a pretreatment step ([0085]), which can be filtration, centrifugation, cycloning, decanting, nanofiltration or microfiltration ([0086]). Microfiltration is preferably performed over membranes having a pore size of 0.1-10 μm ([0087]). As such, insoluble material of a particle size larger than 10 microns is removed. Therefore, claim 20 is rendered obvious.
Regarding claim 24, Habeych teaches the method according to claim 9.
Habeych also teaches that the claimed “fifth” retentate is further treated with a “sixth” cross-flow membrane filtration process whereby the potato protein is concentrated in a “sixth” retentate and the salts migrate through the membrane to create a “sixth” permeate – Analogous to the workflow of instant Figure 4, Habeych teaches that after a diafiltration with a salt solution, the retentate (i.e., second retentate) is subjected to salts removal via “a diafiltration stage against water at lower conductivity, or against regular water, in order to remove salts and isolate native tuber protein essentially free of salt” ([0053]). Habeych further discloses that the ultrafiltered potato fruit juice can be subjected to multiple diafiltration steps ([0156]). As such, Habeych teaches an embodiment where salts are removed from the claimed “fifth” retentate in by using water as the diafiltration solution such that the salts migrate through the membrane, creating a “sixth” permeate and concentrating the proteins in a “sixth” retentate. Therefore, claim 24 is rendered obvious.
Regarding claim 29, Habeych teaches the method according to claim 1.
Habeych also teaches that the conductivity of the first retentate and the second retentate remains within the range of 0.1 to 50 mS/cm during step (ii) and step (iii) – “It has been found that for any solution comprising a native protein isolate as herein defined, it is essential that during the whole isolation process, the conductivity is relatively high. The salt solution against which the diafiltration is performed must have a conductivity of at least 5 mS/cm, and the feed solution must have a conductivity of 2-20 mS/cm.” ([0040]). “Preferably, the conductivity of the solution to be diafiltered (the diafiltration feed solution or feed) remains within the ranges herein specified.” ([0054]). Therefore, claim 29 is rendered obvious.
Regarding claim 33, Habeych teaches the method according to claim 1.
Habeych is silent regarding the absorbance at 600 nm of the first retentate and the second retentate remaining within the range of 0.01 to 100 during step (ii) and (iii).
However, this feature is seen to be an inherent property of the method of Habeych. Regarding inherency, MPEP § 2112(I) states, “‘[T]he discovery of a previously unappreciated property of a prior art composition, or of a scientific explanation for the prior art’s functioning, does not render the old composition patentably new to the discoverer.’ Atlas Powder Co. v. IRECO Inc., 190 F.3d 1342, 1347, 51 USPQ2d 1943, 1947 (Fed. Cir. 1999). Thus the claiming of a new use, new function or unknown property which is inherently present in the prior art does not necessarily make the claim patentable. In re Best, 562 F.2d 1252, 1254, 195 USPQ 430, 433 (CCPA 1977).”
Since the method of Habeych is substantially identical to the claimed method as described regarding claim 1, and the claimed range of 0.01 to 100 is so broad, the claimed absorbance at 600 nm of the first and second retentates in the method of Habeych is seen to be an inherent property. Therefore, claim 33 is rendered obvious.
Regarding claim 35, Habeych teaches the method according to claim 1.
Habeych also teaches that the solubility of the protein in the first retentate and the second retentate remains within the range of 50 % to 99 % relative to the protein soluble in the potato fruit juice or the derivative thereof – Figure 4 of Habeych demonstrates that solubility is maintained above 60 % when the conductivity of the solution protein solution is greater than 1 mS/cm ([0170]-[0172]). Based on these results, Habeych teaches that the conductivity during diafiltration must be maintained above 5 mS/cm ([0173]), such that > 80% of the protein remains soluble (Figure 4). Habeych also teaches “it is essential that during the whole isolation process, the conductivity is relatively high. The salt solution against which the diafiltration is performed must have a conductivity of at least 5 mS/cm, and the feed solution must have a conductivity of 2-20 mS/cm.” ([0040]). “Preferably, the conductivity of the solution to be diafiltered (the diafiltration feed solution or feed) remains within the ranges herein specified.” ([0054]). Since Habeych teaches that the conductivity must remain over 5 mS/cm throughout the process and that at this conductivity, the proteins remain over 80% soluble, claim 35 is rendered obvious.
Regarding claims 41-42, Habeych teaches the method according to claim 9 (re: claim 41) and claim 24 (re: claim 42).
Habeych also teaches that the “fifth” retentate comprises patatin and protease inhibitors, and said method comprises a further step of subjecting the “fifth” retentate to a step of separating patatin from protease inhibitors (re: claim 9), and that the “sixth” retentate comprises patatin and protease inhibitors, and said method comprises a further step of subjecting the “sixth” retentate to a step of separating patatin from protease inhibitors (re: claim 42) – Habeych teaches that “the tuber protein isolate is isolate comprising native protease inhibitor and native patatin. In further much preferred embodiments, the tuber protein isolate is a total native tuber protein isolate.” ([0030]). Since Habeych teaches the method according to claims 9 and 24, and that the isolate comprises patatin and protease inhibitors, it is seen that patatin and protease inhibitors are present in the claimed “fifth” and “sixth” retentates. Habyech further teaches that the diafiltration retentate (which, in this case, corresponds to the “fifth” or “sixth” retenate) or the concentrated solution obtained from ultrafiltering the diafiltration retentate can be subjected to a fractionation step, such as by adsorption or chromatography, which are known methods to separate native tuber protein into a protease inhibitor isolate and a patatin isolate ([0101]). Therefore, claims 41 and 42 are rendered obvious.
Regarding claim 43, Habeych teaches the method according to claim 41.
Habeych also discloses that, while not preferred, the step of separating patatin from protease inhibitors nonetheless can be performed using adsorption techniques, including expanded bed adsorption ([0101]-[0102]). Therefore, claim 43 is rendered obvious.
Claim 22 is rejected under 35 U.S.C. 103 as being unpatentable over Habeych Narvaez et al. (US 2022/0240538 A1) in view of Edens et al. (WO 97/42834).
Regarding claim 22, Habeych teaches the method of claim 1.
Habeych does not teach that the method further comprises the step of continuing the addition of aqueous diafiltration liquid containing one or more salts to the first retentate while continuing the second membrane filtration process in step (iii) until the second retentate contains less than a target amount of the phenolic and/or total glycoalkaloid compounds, whereby the separation of the potato proteins from phenolic and/or total glycoalkaloid compounds has been achieved, wherein the target amount of remaining phenolic and/or total glycoalkaloid compounds in the second retentate corresponds to less than 5000 mg phenolic and/or total glycoalkaloid compounds per kg potato protein on the basis of dry weight.
However, Edens teaches a method for isolating undenatured potato protein from potato fruit juice comprising a pretreatment, concentration by ultrafiltration using a 5 kDa cut-off membrane, and washing by diafiltration in the presence of bisulfite until salts and metal concentrations reach acceptable levels (p. 5, lines 10-28). Membranes with cut-off ranging from 3-100 kDa are disclosed (p. 3, lines 27-29). HPLC analysis of the freeze-dried powder indicated no detectable levels of glycoalkaloids (p. 5, lines 26-27). Thus, Edens teaches that continual diafiltration of the ultrafiltration retentate comprising molecules over 5 kDa reduces the glycoalkaloid amount to levels undetectable by HPLC.
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to apply the diafiltration wash technique of Edens to the method of Habeych as an improved way to remove glycoalkaloids from the potato protein retentate as claimed. See MPEP § 2143(I)(D). First, Habeych teaches the base method of ultrafiltration and diafiltration of potato proteins from potato fruit juice as described regarding claim 1 above. Habeych teaches that glycoalkaloids can be removed at any step, and that glycoalkaloid extraction is performed by other known techniques, such as adsorption ([0092]) to reach at most 200 mg/kg glycoalkaloids ([0091]). Edens teaches the applicable known technique of continual diafiltration to wash away non-protein components, including glycoalkaloids, such that the final amount of glycoalkaloids in the protein product is undetectable by HPLC (p. 5, lines 21-28). Since Habeych teaches the reduction of glycoalkaloids to at most 200 mg/kg, one of ordinary skill in the art would have recognized that applying the technique of Edens would have yielded predictable results and resulted in an improved system by eliminating the need for an additional adsorption step to remove glycoalkaloids. Therefore, claim 22 is rendered obvious.
Claims 34 and 37 are rejected under 35 U.S.C. 103 as being unpatentable over Habeych Narvaez et al. (US 2022/0240538 A1) in view of Garidel et al. (Garidel, P., Kuhn, A.B., Schäfer, L.V., Karow-Zwick, A.R., and Blech, M. (2017). High-concentration protein formulations: How high is high?. Eur J Pharm Biopharm, 119, pp. 353-60. https://doi.org/10.1016/j.ejpb.2017.06.029).
Regarding claims 34 and 37, Habeych teaches the method according to claim 1.
Habeych is silent regarding the true protein concentration of the first retentate (re: claim 34) and second retentate (re: claim 37) is in the range of 8 g/L to 180 g/L.
However, Garidel discloses monoclonal antibody (i.e., native protein) drug formulations at high concentrations ranging between 50 and 150 mg/mL (i.e., g/L), and that formulations at these concentrations have specific solution, stability, and colloidal properties that differ from formulations at a low protein concentration (e.g., at 10 mg/mL) (p. 353, Abstract). Garidel teaches challenges associated with high-concentration protein formulations, stating that protein solubility and solution properties are key factors at high concentrations, and “at high protein concentration >100 mg/ml, the solution becomes crowed and protein-protein interactions become more relevant. As a consequence of increased protein concentration, opalescence and especially viscosity may strongly increase.” (p. 354, col. 1, ¶ 4). Garidel further discloses that ultrafiltration/diafiltration (UF/DF) is the most used and appropriate method for concentrating proteins, however “the strong, non-linear dependence of viscosity on protein concentration sets limits to the application range of UF/DF procedures. The high viscosity induces strong backpressures in the UF/DF systems and the filtration flow is strongly reduced, thus making the process challenging to develop.” (p. 354, col. 2, ¶ 4).
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to modify the method of Habeych with the teachings of Garidel to ensure that the true protein concentration of the first and second retentates is in the range of 8 g/L to 180 g/L as claimed. First, Habeych teaches that the proteins are isolated in the native form and are isolated via ultrafiltration/diafiltration. Garidel teaches that at protein concentrations >100 mg/mL, viscosity may strongly increase (p. 354, col. 1, ¶ 4) and the increased viscosity makes UF/DF challenging (p. 354, col. 2, ¶ 4). Therefore, one of ordinary skill in the art would have been motivated to keep the protein concentration of the retentates below 100 mg/mL, and closer to the disclosed lower protein concentration of 10 mg/mL (p. 353, Abstract) in the ultrafiltration and diafiltration processes of Habeych to maintain a viscosity that permits successful filtration processes, and for the same reasons would have had a reasonable expectation of success given the teachings of Garidel. Therefore, claims 34 and 37 are rendered obvious.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1 and 2 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 28 and 29 of copending Application No. 18/001,271 (hereinafter ‘271) in view of Habeych Narvaez et al. (US 2022/0240538 A1).
Regarding claim 1, claim 28 of ‘271 teaches a method for separation of (a) potato proteins from (b) first salts and phenolic and/or glycoalkaloid compounds in potato fruit juice or a derivative thereof, said method comprising the steps of:
(i) providing a potato fruit juice or a derivative thereof, comprising:
potato proteins; and
one or more first salts; and
phenolic and/or glycoalkaloid compounds;
(ii) subjecting said potato fruit juice or the derivative thereof to a first cross-flow membrane filtration process wherein water and at least a portion of the first salts and at least a portion of the phenolic and/or glycoalkaloid compounds migrate across the membrane into a first permeate and wherein the potato proteins are retained in a first retentate;
(iii) subjecting the first retentate to a second cross-flow membrane filtration as diafiltration, to create a second permeate being a diafiltrate containing at least a portion of said phenolic and/or glycoalkaloid compounds and salts and a second retentate comprising potato proteins and salts;
said method further comprising a step of eliminating or reducing enzymatic activity by exposing:
the first retentate obtained in step (ii) prior to step (iii); or
the second retentate obtained in step (iii); or
any other aqueous stream comprising potato proteins obtained downstream of step (iii),
to pH values between 2.0 and 4.5 in a time and temperature interval sufficient to eliminate or reduce unwanted enzymatic activity of the potato proteins without adversely affecting functionality of the potato proteins.
Claim 1 differs from ‘271 claim 28 in that claim 28 does not teach that the potato proteins comprise patatin and protease inhibitor; adding aqueous diafiltration liquid containing one or more salts to the first retentate obtained in step (ii) to form a diluted first retentate having a conductivity of between 1 mS/cm and 50 mS/cm and subjecting said diluted first retentate to a second cross-flow membrane filtration as diafiltration, wherein the pH of the first retentate and the second retentate remains within the range of 4.5 to 8.5 during step (ii) and step (iii); and increasing the pH to a value between 4.5 and 8.5 after eliminating or reducing unwanted enzymatic activity of the potato proteins without adversely affecting functionality of the potato proteins.
However, Habeych teaches that the potato proteins comprise patatin and protease inhibitor – tuber processing water, for example potato fruit juice as obtained after starch isolation ([0067]), was used as raw material for production of a total native (potato) protein isolate ([0137]). A total isolate comprises protease inhibitor and patatin ([0031]).
Habeych also teaches (iii) adding aqueous diafiltration liquid containing one or more salts to the first retentate obtained in step (ii) to form a diluted first retentate having a conductivity of between 1 mS/cm and 50 mS/cm and subjecting said diluted first retentate to a second cross-flow membrane filtration as diafiltration, to create a second permeate being a diafiltrate containing at least a portion of said phenolic and/or glycoalkaloid compounds and salts and a second retentate comprising potato proteins, and salts – “The retentate from the ultrafiltration [i.e., first retentate] was subjected to further treatment comprising diafiltration against a salt solution having 0.33 or 50.66 [sic, 0.66] wt. % NaCl [i.e., one or more salts]…This resulted in a potato protein isolate solution [i.e., second retentate].” ([0144]). “Each diafiltration step entails dilution of protein solution volume VPJ with diafiltration volume VDF in a ratio as indicated and concentrating the diluted protein solution back to the original volume by ultrafiltration.” ([0152]). “[I]t is essential that during the whole isolation process, the conductivity is relatively high. The salt solution against which the diafiltration is performed must have a conductivity of at least 5 mS/cm, and the feed solution must have a conductivity of 2-20 mS/cm.” ([0040]). “Preferably, the conductivity of the solution to be diafiltered (the diafiltration feed solution or feed) remains within the ranges herein specified.” ([0054]); and
wherein the pH of the first retentate and the second retentate remains within the range of 4.5 to 8.5 during step (ii) and step (iii) – the pH of the diafiltration feed solution (e.g., from step (ii)) is preferably 5.5-7.0 ([0044]). “Preferably in this embodiment, the pH remains the same throughout all diafiltration stages.” (0054]). “In further preferred embodiments, the salt solution may have a pH of…5.5-8.0…In preferred embodiments, this pH is maintained throughout the diafiltration.” ([0050]). Since the pH of both the diafiltration feed solution and the salt solution are within the claimed range throughout the diafiltration process, the pH of the first and second retentates would also be within the claimed range.
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to have modified the method as presented in ‘271 claim 28 with the teachings of Habeych to maintain protein solubility and flux through the filtration membrane in preparing a total potato protein isolate (comprising patatin and protease inhibitors). One of ordinary skill in the art would have been motivated to apply these teachings and have a reasonable expectation of success for doing so because Habeych teaches that a salt solution having a conductivity of at least 5 mS/cm (and a preferred pH in the range of 5.5-8.0 ([0050])) stabilizes the protein during the mechanical stress that comes with diafiltration, thereby maintaining and even increasing protein solubility under mechanical stress, increasing flux stability and diafiltration operation time, and minimizing protein loss ([0042]), and one of ordinary skill in the art would have been motivated to isolate useful proteins from the potato processing water, including patatin and protease inhibitors as taught by Habeych.
Where Habeych renders obvious a pH in the range of 4.5 to 8.5 during step (ii) and step (iii), the pH is necessarily increased to a value between 4.5 and 8.5 after eliminating or reducing unwanted enzymatic activity of the potato proteins without adversely affecting functionality of the potato proteins between steps (ii) and (iii).
Therefore, the instant claim 1 is rendered obvious in view of ‘271 claim 28 and Habeych.
Regarding claim 2, claim 28 of ‘271 and Habeych teach all limitations of claim 1.
Claim 29 of ‘271 teaches that the first retentate obtained in step (ii) prior to step (iii), the second retentate obtained in step (iii), or any other aqueous stream comprising potato proteins and optionally insoluble fibers obtained downstream of step (iii) is exposed to:
a pH value between 2.0 and 4.5;
a temperature in the range of 1-70 °C; and
in a time span of up to 240 minutes.
Therefore, claim 2 is rendered obvious in view of ‘271 claim 29 and Habeych as described regarding claim 1 above.
This is a provisional nonstatutory double patenting rejection.
Claims 1 and 2 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 34 and 35 of copending Application No. 18/001,290 (hereinafter ‘290) in view of Habeych Narvaez et al. (US 2022/0240538 A1).
Regarding claim 1, claim 34 of ‘290 teaches a method for separation of (a) potato proteins and insoluble fibers from (b) first salts and phenolic and/or glycoalkaloid compounds in potato fruit juice or a derivative thereof, said method comprising the steps of:
(i) providing a potato fruit juice or a derivative thereof, comprising:
potato proteins; and
one or more first salts; and
phenolic and/or glycoalkaloid compounds; and
insoluble fibers;
(ii) subjecting said potato fruit juice or the derivative thereof to a first cross-flow membrane filtration process wherein water and at least a portion of the first salts and at least a portion of the phenolic and/or glycoalkaloid compounds migrate across the membrane into a first permeate and wherein the potato proteins are retained in a first retentate;
(iii) adding aqueous diafiltration liquid containing one or more salts to the first retentate obtained in step (ii) to form a diluted first retentate having a conductivity of between 1 mS/cm and 50 mS/cm and subjecting said diluted first retentate to a second cross-flow membrane filtration as diafiltration, to create a second permeate being a diafiltrate containing at least a portion of said phenolic and/or glycoalkaloid compounds and salts and a second retentate comprising potato proteins, salts and insoluble fibers;
said method further comprising a step of eliminating or reducing enzymatic activity by exposing:
the first retentate obtained in step (ii) prior to step (iii); or
the second retentate obtained in step (iii); or
any other aqueous stream comprising potato proteins with insoluble fibers obtained downstream of step (iii),
to pH values between 2.0 and 4.5 in a time and temperature interval sufficient to eliminate or reduce unwanted enzymatic activity of the potato proteins without adversely affecting functionality of the potato proteins.
Claim 1 differs from ‘290 claim 34 in that claim 34 does not teach that the potato proteins comprise patatin and protease inhibitor; the pH of the first retentate and the second retentate remains within the range of 4.5 to 8.5 during step (ii) and step (iii); and increasing the pH to a value between 4.5 and 8.5 after eliminating or reducing unwanted enzymatic activity of the potato proteins without adversely affecting functionality of the potato proteins.
However, Habeych teaches that the potato proteins comprise patatin and protease inhibitor – tuber processing water, for example potato fruit juice as obtained after starch isolation ([0067]), was used as raw material for production of a total native (potato) protein isolate ([0137]). A total isolate comprises protease inhibitor and patatin ([0031]).
Habeych also teaches that the pH of the first retentate and the second retentate remains within the range of 4.5 to 8.5 during step (ii) and step (iii) – the pH of the diafiltration feed solution (e.g., from step (ii)) is preferably 5.5-7.0 ([0044]). “Preferably in this embodiment, the pH remains the same throughout all diafiltration stages.” (0054]). “In further preferred embodiments, the salt solution may have a pH of…5.5-8.0…In preferred embodiments, this pH is maintained throughout the diafiltration.” ([0050]). Since the pH of both the diafiltration feed solution and the salt solution are within the claimed range throughout the diafiltration process, the pH of the first and second retentates would also be within the claimed range.
It would have been obvious for one of ordinary skill in the art, before the effective filing date of the claimed invention, to have modified the method as presented in ‘290 claim 34 with the teachings of Habeych to maintain protein solubility and flux through the filtration membrane in preparing a total potato protein isolate (comprising patatin and protease inhibitors). One of ordinary skill in the art would have been motivated to apply these teachings and have a reasonable expectation of success for doing so because Habeych teaches that a salt solution having a conductivity of at least 5 mS/cm (and a preferred pH in the range of 5.5-8.0 ([0050])) stabilizes the protein during the mechanical stress that comes with diafiltration, thereby maintaining and even increasing protein solubility under mechanical stress, increasing flux stability and diafiltration operation time, and minimizing protein loss ([0042]). One of ordinary skill in the art would have been motivated to isolate useful proteins from the potato processing water, including patatin and protease inhibitors as taught by Habeych.
Where Habeych renders obvious a pH in the range of 4.5 to 8.5 during step (ii) and step (iii), the pH is necessarily increased to a value between 4.5 and 8.5 after eliminating or reducing unwanted enzymatic activity of the potato proteins without adversely affecting functionality of the potato proteins between steps (ii) and (iii).
Therefore, the instant claim 1 is rendered obvious in view of ‘290 claim 34 and Habeych.
Regarding claim 2, claim 35 of ‘290 and Habeych teach all limitations of claim 1.
Claim 35 of ‘290 teaches that the first retentate obtained in step (ii) prior to step (iii), the second retentate obtained in step (iii), or any other aqueous stream comprising potato proteins and optionally insoluble fibers obtained downstream of step (iii) is exposed to:
a pH value between 2.0 and 4.5;
a temperature in the range of 1-70 °C; and
in a time span of up to 240 minutes.
Therefore, claim 2 is rendered obvious in view of ‘290 claim 35 and Habeych as described regarding claim 1 above.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Claim Rejections – 35 U.S.C. § 103: Applicant’s arguments filed on 2 February 2026 have been fully considered, but they are not persuasive.
Applicant first argued that amended claim 1 now requires that the potato proteins comprise both patatin and protease inhibitor, and pH adjustment in Habeych is used to precipitate and remove patatin in order to enrich protease inhibitor content (p. 7, ¶ 6). Applicant referenced Example 5 of Habeych, in which a substantial amount of patatin is precipitated and removed, resulting in a final product with 90% protease inhibitor content (Id.). Applicant argued that amended claim 1 now requires that after the lo-pH treatment to eliminate or reduce enzymatic activity, the pH is increased again to a value of between 4.5 and 8.5, and Habeych does not teach or suggest increasing the pH back to 4.5 to 8.5 after the low-pH treatment while maintaining both patatin and protease inhibitor in the product (p. 7, ¶ 7 – p. 8, ¶ 2).
Applicant’s arguments have been considered, but they are not persuasive. Habeych does not disclose that the entirety of the patatin proteins is removed, and as such, a small amount of patatin proteins can remain in the non-precipitated fraction, thereby meeting the claimed limitation of potato proteins comprising patatin and protease inhibitor. Applicant references Example 5 in Habeych (Arguments, p. 7, ¶ 6 – p.8, ¶ 1). This is but one example falling within the scope of the disclosure. As indicated in the rejection, Habeych discloses a pH adjustment in the range of 4.0-5.5 to precipitate at least part of the patatin fraction, enriching the relative quantity of native protease inhibitor ([0082]). As such, Habeych does not necessarily teach removal of all patatin, and describes the process as “increasing the relative quantity of protease inhibitor” ([0082]). Habeych discloses a step of reducing the pH to a range of 4.0-5.5 overlapping the claimed range of 2.0-4.5. After treatment, the diafiltration step is carried out at a pH from 5.5-8.0 ([0050]) and the pH is held constant throughout the diafiltration step ([0054]). Therefore, Habeych discloses temporarily lowering the pH of the first retentate comprising potato proteins, and increasing the pH to a value between 4.5 and 8.5, as claimed.
As provided by MPEP § 2145(II), “[m]ere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention. In re Wiseman, 596 F.2d 1019, 201 USPQ 658 (CCPA 1979)”, and “‘[t]he fact that appellant has recognized another advantage which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious.’ Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985)”.
Since Habeych teaches the step of temporarily lowering the pH of the first retentate in ranges that render the claim obvious as described here and in the rejection of claim 1, the recognition that such a treatment also has the claimed effect on eliminating or reducing unwanted enzyme activity of the potato proteins without adversely affecting functionality of the potato proteins does not render the claim non-obvious. Therefore, Applicant’s argument is not found to be persuasive.
Additionally, Habeych discloses said method further comprising a step of eliminating or reducing enzymatic activity by exposing:
the second retentate obtained in step (iii); or
any other aqueous stream comprising potato proteins and optionally insoluble fibers obtained downstream of step (iii),
to pH values between 2.0 and 4.5 in a time and temperature interval sufficient to eliminate or reduce unwanted enzymatic activity of the potato proteins without adversely affecting functionality of the potato proteins, whereafter the pH is increased again to a value between 4.5 and 8.5.
Applicant is directed to the rejection of this limitation in paragraphs 20-25 hereinabove.
Regarding claims 22, 34, and 37, Applicant argued that since amended claim 1 is patentable, these claims are also patentable (p. 8, ¶¶ 4-5).
Where Applicant’s arguments toward claim 1 are not persuasive, neither are Applicant’s arguments regarding claims 22, 34, and 37.
For at least these reasons, Applicant’s arguments are not found to be persuasive, and the claims are rejected under 35 U.S.C. § 103 as presented hereinabove.
Double Patenting:
Applicant makes no substantive arguments concerning the double patenting rejections (p. 8, ¶ 6 – p. 9, ¶ 1). Applicant’s acknowledgement and deferral of filing a terminal disclaimer until such a time as the present application or at least subject matter therein is indicated to be allowable is acknowledged.
Conclusion
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure:
Van Koningsveld et al. 2006 (Van Koningsveld, G. A., Walstra, P., Voragen, A. G., Kuijpers, I. J., Van Boekel, M. A., & Gruppen, H. (2006). Effects of protein composition and enzymatic activity on formation and properties of potato protein stabilized emulsions. Journal of Agricultural and Food Chemistry, 54(17), 6419-6427.) discusses removing lipolytic activity of patatin for stabilizing emulsions. Potato proteins are treated at pH 3, and then shifted to pH 7.
Van Koningsveld et al. 2001 (Van Koningsveld, G. A., Gruppen, H., de Jongh, H. H., Wijngaards, G., van Boekel, M. A., Walstra, P., & Voragen, A. G. (2001). Effects of pH and heat treatments on the structure and solubility of potato proteins in different preparations. Journal of Agricultural and Food Chemistry, 49(10), 4889-4897.) discusses pH- and thermal stability of patatin.
Ralet et al. (Ralet, M. C., & Guéguen, J. (2000). Fractionation of potato proteins: solubility, thermal coagulation and emulsifying properties. LWT-Food Science and Technology, 33(5), 380-387.) discusses stability of patatin.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to James Shellhammer whose telephone number is (703) 756-5525. The examiner can normally be reached Monday - Thursday 7:30 am - 5:00 pm ET.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Emily Le can be reached at (571) 272-0903. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/JAMES P. SHELLHAMMER/Examiner, Art Unit 1793
/EMILY M LE/Supervisory Patent Examiner, Art Unit 1793
Prosecution Insights