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 .
DETAILED OFFICE ACTION
This Office Action is in response to the papers filed on 18 March 2026.
PRIORITY
Applicant claims priority to FR1455466. A certified translation has not been provided. PCT/FR2015/051581 filed on 06/15/2015 is acknowledged.
CLAIMS UNDER EXAMINATION
Claims 11 and 16-21 have been examined on their merits.
REJECTIONS
The ranges recited in claim 11 have been amended. The rejections have been modified to address the claim limitations.
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 11 and 16-21 are rejected under 35 U.S.C. 103 as being unpatentable over Fouache et al. (previously cited; Method Of Manufacturing A Maltose-Rich Syrup Patent 6284498 2001) in view of Nuofang et al. (previously cited; A method For Extracting β-amylase from Soybean. CN102965358 13 March 2013), Upadhyah et al. (previously cited; A protocol For Optimal Extraction and Stabilization of Barley Amylase (Biotechnology Techniques Vol 4 No 2 117-120 1990) and Bergmans et al. (previously cited; Liquid Bread Improving Compositions. US2003190399A1) as evidenced by Stevenson et al. (previously cited; Structures and Functional Properties of Starch From Seeds of Three Soybean (Glycine max (L.) Merr.) Varieties*, Starch/Stärke 58 (2006) 509–519).
Fouache et al. teach a method of manufacturing a maltose-rich syrup (Abstract). The syrup has a maltose content higher than 80% (see claim 1 of Fouache). Fouache teaches carrying out a liquefaction of a starch milk, carrying out a saccharification of the liquefied starch milk in the presence of a maltogenic α-amylase; continuing the saccharification of the liquefied starch milk in the presence of a β-amylase and at least one debranching enzyme to obtain a syrup which is rich in maltose (column 2, lines 20-33).
Fouache teaches the following (Example 1):
A starch milk, with 31% dry matter, is liquefied in standard fashion with the aid of 0.2% TERMAMYLR 120L (α-amylase marketed by the firm NOVO) to a pH of 5.7 to 6.5 up to a DE slightly below 4. Then the reaction medium is heated for a few seconds at 140° C. so as to inhibit the α-amylase, then the pH is adjusted between 5 and 5.5 and the temperature adjusted to 55° C. The saccharification is carried out to a dry matter of 25%, or slightly less, first of all in the presence of pullulanase (PULLUZYMER 750L marketed by the firm ABM) and of maltogenic (α-amylase (MALTOGENASER 4000L marketed by the firm NOVO) at respective doses of 0.1% and 0.3% of the dry matter.
Therefore Fouache teaches liquefying a starch milk with an α-amylase at a pH of 5.7 to 6.5 to obtain a liquefied starch milk. The instant specification states heating to 140° C inhibits alpha-amylase ([0079]). Because the art teaches this condition, it is interpreted to inhibit the liquefied milk. Fouache teaches adjusting the liquified starch milk to a pH of between 5 and 5.5.
After having let the α-amylase act, the next step is the saccharification of the liquefied starch milk by means of a β-amylase such as that marketed by the firm GENECOR under the designation of SPEZYME BBA 1500 (see column 3, lines 54-57).
The deficiency of Fouache is:
Fouache is silent regarding the formulation of the β-amylase used in the method.
Nuofang et al. is directed to a method of obtaining and formulating a liquid β-amylase (Abstract). β-amylase is formulated by adding a stabilizer ([0015]). Preferably, the stabilizer comprises 5-10% glycerin, 0.5% potassium sorbate and 1% trehalose ([0020]). It is well known in the art that “glycerin” is a synonym for “glycerol”. Nuofang teaches β-amylase is a commercially significant enzyme in the starch industry which is used to produce maltose, which is used in the food industries ([0004]).
Upadhyah teaches β-amylase is used for the saccharification of liquefied starch (first paragraph of introduction). Upadhyah analyzes storage stability of liquid state β-amylase with 0.5% sodium carbonate as a stabilizer (page 117, first paragraph; Figure 1, 6B; page 118 “Stabilization of β-amylase”). The art teaches the chemical stabilized around 50% of the original activity (see page 120, second paragraph).
Bergmans et al. teach a composition comprising one or more enzymes and one or more polyol ([0008]). β-amylase is a preferred enzyme ([0013]). Glycerol is a polyol ([0010]). Polyols provide a stabilizing effect ([0013]). Bergmans teaches 25-65% polyol ([0010]). The composition is storage stable ([0008]).
It would have been obvious to combine the teachings of the prior art by using sodium carbonate in the aqueous stabilizer taught by Nuofang. Fouache teaches a composition comprising β-amylase and Nuofang and Upadhyah teach potassium sorbate, glycerol and sodium carbonate are β-amylase stabilizers. One would combine known stabilizers to improve enzyme stability. See In re Kerkoven. One would have had a reasonable expectation of success since the prior art teaches potassium sorbate, glycerol and sodium carbonate can be used to stabilize β-amylase. One would have expected similar results since each reference is directed to starch-degrading enzymes.
It would have been obvious to optimize the amounts of potassium sorbate, glycerol and sodium carbonate. Nuofang stabilizes β-amylase with 0.5% potassium sorbate. Upadhyay uses 0.5% sodium carbonate to stabilize β-amylase. Therefore the stabilizers are expected to have the same properties as the claimed amount. The MPEP teaches “a prima facie case of obviousness exists where the claimed ranges and prior art ranges do not overlap but are close enough that one skilled in the art would have expected them to have the same properties. One of ordinary skill would optimize the amount of each stabilizer to achieve the desired enzyme stability.
Nuofang teaches 5-10% glycerol. Bergmans teaches 25-65% glycerol can be used to stabilize β-amylase. Bergmans teaches 25-65% glycerol can be used as a stabilizer. One would optimize the amount of glycerol based on the amount of enzyme present. The skilled artisan would do so to provide the desired stability. The skilled artisan would have had a reasonable expectation of success since Bergmans teaches the amount of polyol used as a stabilizer can be optimized. See MPEP 2144.05(I)(II).Therefore claim 11 is rendered obvious.
Regarding claim 16: Nuofang teaches 0.5% potassium sorbate. Bergmans teaches 25-65% glycerol. Upadhyay uses 0.5% sodium carbonate. Thus, these amounts read on “about” since the specification does not define the term. One of ordinary skill would optimize the amount of each stabilizer to achieve the desired enzyme stability.
Claim 16 is included in this rejection.
Nuofang teaches β-amylase is obtained from soybean ([0001] [0008]). Soybean is a plant. Water is added to produce a slurry ([0009]). The slurry is extracted ([0010]), the slurry-residue is separated ([0011], the slurry is precipitated ([0012]) and the enzyme is obtained from a clarified, filtered supernatant solution ([0013] [0014]). As evidenced by Stevenson, soybean contains starch (Introduction, right column, first paragraph).Therefore the enzyme is obtained from the soluble (solution) fraction of a soybean (hence, starch) plant. Therefore claim 20 is included in this rejection.
As set forth above, Nuofang provides a soluble fraction of a starch plant. The art
teaches filtration using a 200-300 mesh (hence, microfiltration ([0011]) and an
ultrafiltration ([0014]). Therefore claim 21 is included in this rejection.
Therefore Applicant’s Invention is rendered obvious as claimed.
Claims 17-19 are rejected under 35 U.S.C. 103 as being unpatentable over Fouache et al., Nuofang et al., Upadhyay et al. and Bergman as set forth in the rejection of claim 11 above, and further in view of Beals et al. (previously cited; Enzymes And the Rate Of Chemical Reactions. 1999, pages 1-3).
Claim 11 is rejected on the grounds set forth above. The teachings of the prior art are reiterated. Fouache et al. teach β-amylase (supra). The art discloses the use of 0.05% SPEZYME in Example 1. Uphadyay adds stabilizers to a 500 ml aliquot of β-amylase (see page 118, third paragraph). The β-amylase has a specific activity of 33.3 Units/mg (Table 1)
The references do not teach the percentage of β-amylase as recited in claim 17.
Beals et al. teach the rate of a chemical reaction is affected by the amount of enzyme
and substrate (page 1, second paragraph). The art teaches the maximum reaction rate
(Vmax) is directly proportional to the total enzyme concentration (last paragraph of page
1).
It would have been obvious to optimize the amount of β-amylase added to a
composition that is used to digest starch. One would have been motivated to do so since Fouache uses β-amylase for starch digestion and Beals teaches the rate of digestion is directly proportional to the amount of enzyme that is present. Because the amount enzyme affects the rate of reaction, it is interpreted to be a result effective variable. The skilled artisan would increase the amount of β-amylase present to increase the rate of reaction. The MPEP teaches generally, differences in concentration do not support patentability absent evidence of criticality. One would have expected similar results because each reference is directed to an enzyme composition that can be used to treat substrates containing starch. Therefore claims 17-19 are included in this rejection.
Therefore Applicant’s Invention is rendered obvious as claimed.
37 CFR 1.132 Declaration
The Examiner acknowledges receipt of the Declaration under 37 CFR 1.132 by Dr. Guillaume Fardin filed on 18 March 2026. The Declaration states the ranges recited in amended claim 11 are critical when combined. The Declarant states it is his opinion Tables 1, 1a and 2 of the specification demonstrate the claimed ingredients produce the best degree of stability when combined in the claimed ranges.
Argument 1: Regarding the amount of glycerol: The Declaration states glycerol cannot be used alone as a stabilizer (see page 6, “Example 1” of Declaration, see Table 2). The Declaration acknowledges the data demonstrates “increasing the concentration of glycerol alone may improve the stability of β-amylase” (see 50% glycerol), but states when additional components are added the composition becomes “more complex” and unpredictable and does not make it possible to achieve “the satisfactory degree of stability of the β-amylase as stated at [0076] of the Specification”.
In response: None of the rejections are not based on the use of glycerol alone. While the arguments are directed to a “satisfactory degree” of enzyme stability in the specification, this is not a claim limitation. The claims are directed to producing maltose or maltose syrup with a maltose content higher than 80% by weight. The experiments in Table 2 do not demonstrate criticality of the claimed composition for production of maltose.
Regarding Table 1a: “Cocktail 5” demonstrates increased enzyme stability at 90 days when 40% glycerol, 0.2% potassium sorbate (PS) and 0.2% Na2CO3 are combined. Claim 11 encompasses 35-45% glycerol, 0.1-0.3% PS and 0.1-0.% Na2CO3. None of the experiments in the Declaration demonstrate criticality when the claimed components are combined in amounts encompassed by claim 11.
Argument 2: Regarding sodium carbonate: The Declaration states replacing sodium carbonate with another sodium salt (disodium hydrogen phosphate or calcium carbonate) does not lead to the same stabilization properties. The Declaration states a 5% improvement (relative to other compositions) is achieved when 40% glycerol, 0.2% potassium sorbate and 1% Na2CO3 is used (composition 3 of Table 1 on page 8) when compared to 50% glycerol, 0.2% potassium sorbate and 1% disodium hydrogen phosphate.
In response: The composition in Table 1 (page 8) which provides increased stability comprises 40% glycerol, 0.2% potassium sorbate and 1% Na2CO3 (sodium carbonate). This is not commensurate with the scope of claim 11, which recites 0.1-0.3% sodium carbonate. The argument of criticality is not persuasive because Table 1 indicates a higher amount of sodium carbonate can be used to achieve increased stability. The experiments in the table do not demonstrate criticality in producing maltose syrup with the claimed maltose content.
Argument 3: Regarding Part II (page 12 of Declaration), the Declaration states Table 1a demonstrates the claimed concentrations of components are critical (cocktail 5).
In response: Table 1a demonstrates improved enzyme stability when 40% glycerol, 0.2% PS and 0.2% Na2CO3 are combined. Claim 11 encompasses 35-45% glycerol, 0.1-0.3% PS and 0.1-0.3% Na2CO3. None of the experiments demonstrate criticality commensurate with the scope of components recited in claim 11. None of the experiments disclose criticality in producing maltose or maltose syrup with at least 80% maltose as recited in the preamble of claim 11.
Argument 4: Regarding Part III (page 15 of Declaration), the Declaration states the cocktail in “Ex 1” of Table A demonstrates increased maltose content.
In response: The cocktail in “Ex 1” comprises 40% glycerol, 0.2% PS and 0.2% Na2CO3 are combined. Claim 11 encompasses 35-45% glycerol, 0.1-0.3% PS and 0.1-0.3% Na2CO3. None of the experiments demonstrate criticality commensurate with the scope of components recited in claim 11. None of the experiments disclose criticality in producing maltose or maltose syrup with at least 80% maltose as recited in the preamble of claim 11.
Affidavits or declarations are provided as evidence and must set forth facts, not merely conclusions. In re Pike and Morris, 84 USPQ 235 (CCPA 1949).
Upon consideration of the facts taught by the prior art and the information submitted by the Affiant, the balance of evidence indicates that the prior art teaches the instantly claimed inventions.
APPLICANT’S ARGUMENTS
The arguments made in the response filed on 18 March 2026 are acknowledged. Claim
11 has been amended to incorporate the limitations previously recited in claim 15:
from 0.1 to 0.3% potassium sorbate; from 35 to 45% glycerol; and from 0.1 to 0.3% sodium carbonate. The Applicant argues criticality of the claimed ranges.
Argument 1: The Applicant argues the skilled artisan could not have expected that replacing trehalose with sodium carbonate would have improved the stabilization of the ß-amylase and maltose yield. The arguments state the Declaration demonstrate why sodium carbonate cannot be replaced.
Response to Argument 1: Applicant’s arguments are directed to the previous rejections. The rejections have been modified to address the amounts now recited in claim 11.
None of the rejections are based on replacing trehalose with sodium carbonate. Claim 11 recites a composition “containing” potassium sorbate, glycerol and sodium carbonate. The transitional phrase “comprising”, which is synonymous with “containing”
is inclusive or open-ended and does not exclude additional, unrecited elements or method steps (See MPEP 2113.03). Nuofang teaches a composition for stabilizing β-amylase. Nuofang teaches glycerol and potassium sorbate are used to stabilize β-amylase. The rejection of claim 11 acknowledges Nuofang does not teach sodium carbonate. The rejection addressed why it would be obvious to use ingredients known to stabilize β-amylase in a composition which stabilizes β-amylase. Upadhyah identifies sodium carbonate as a β-amylase stabilizer.
The Declaration has been considered above. The Declaration discloses experiments that replace sodium carbonate with other salts (Na₂HPO₄ and CaCO₃). Examiner reiterates the rejection is not based on replacing trehalose with another salt. Upadhyah identifies sodium carbonate as a β-amylase stabilizer.
The Applicant states small differences make a critical difference. Claim 11 encompasses a range, but the declaration only provides evidence of one data point within the claimed range: 40% glycerol, 0.2% potassium sorbate and 0.2% sodium carbonate exhibiting increased stability. It is unclear whether all data points within the claimed range produce the effect argued by the Applicant.
Argument 2: The Applicant argues the skilled artisan could not have expected that modifying the concentration of glycerol would have improved the stabilization of the β-amylase and maltose yield. The Applicant argues Nuofang teaches “a low glycerol content” while Bergmans teaches a “much higher glycerol content”. The Applicant argues Bergmans does not specifically refer to β-amylase stabilization and refers to compositions having “a very low enzyme content”. There is no motivation for the
skilled artisan to change the concentration of glycerol of NUOFANG et al. The Applicant argues Bergman teaches the use of a “polyol”, and not all polyols can stabilize β-amylase. The Applicant argues even if the skilled artisan had considered the use of glycerol as the most appropriate polyol to stabilize β-amylase, the Applicant submits that he/she would not have achieved a satisfactory degree of enzyme stability.
The Applicant argues the Declaration demonstrates increased glycerol does not make it possible to achieve the satisfactory degree of stability of the β-amylase
Response to Argument 2: The Declaration does not demonstrate increased glycerol does not achieve satisfactory stability, as argued by the Applicant. The Declaration demonstrates 50% glycerol, which is outside the claimed range, produces the highest stability (see Table 2, page 6 of Declaration). This is acknowledged in the Declaration.
Bergmans is not relied upon to teach glycerol. Nuofang teaches 5-10% glycerin (glycerol). Nuofang never requires using a “low glycerol content”, as stated by the Applicant. The phrase does not appear in Nuofang. Nuofang does not teach the amount of glycerol cannot be optimized. Bergmans et al. teach a composition comprising an enzyme and a polyol ([0008]). β-amylase is a preferred enzyme ([0013]). The art teaches polyols provide a “stabilizing effect”. The composition is storage stable ([0008]). Glycerol is identified as a polyol ([0010]). Bergmans teaches 25-65% polyol ([0010]).
While the Applicant argues one “would not have achieved a satisfactory degree of enzyme stability”, the claims are not directed to a specific degree of enzymatic activity. Claim 11 is directed to a method of producing a maltose/maltose syrup with a maltose content higher than 80%. No evidence has been provided demonstrating criticality of a composition comprising each component in the claimed range. The experiments performed with only glycerol are not commensurate with the scope of claim 11.
Argument 3: The Applicant argues the Declaration demonstrates even a small variation in the concentration of potassium sorbate can have a significant impact on the stabilization of ß-amylase and maltose production. The arguments state a concentration of 0.2% results in increased residual β-amylase activity and maltose content.
Response to Argument 3: Table 1a (page 7) of the Declaration compares 0.2% and 0.4% potassium sorbate (“cocktail 4” and “cocktail 5”). The cocktails produce 60% and 54% stability, respectively, at day 90. While increased stability is observed at 0.2%, this is not commensurate with the scope of claim. The Declaration states the effect becomes unpredictable when ingredients are combined. The Applicant argues even a small variation in ingredient amounts can have a large variation. No evidence has been provided demonstrating the effect when 0.1-0.3% potassium sorbate is used. Therefore it is unclear if all of the amounts encompassed by the claims are critical. The arguments are not persuasive.
Argument 4: The Applicant argues a sufficient number of data points inside and outside of the claimed composition demonstrates criticality.
Response to Argument 4: In Table 2 (page 6): the experiments only use glycerol. The data demonstrates 50% glycerol, which is outside the claimed amount of glycerol, produces the highest enzyme stability. This data does not demonstrate criticality of the claimed amount of glycerol. Table 1a (“cocktail 5” page 7) demonstrates increased stability is observed with 40% glycerol, 0.2% potassium sorbate and 0.2% sodium carbonate. The Declaration states the claimed components and concentrations are critical, but the effect is only observed at these concentrations. The arguments are not persuasive.
CONCLUSION
No Claims Are Allowed
Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to NATALIE MOSS whose telephone number is (571) 270-7439. The examiner can normally be reached on Monday-Friday, 8am-5pm EST.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Sharmila Landau can be reached on (571) 272-0614. The fax phone number for the organization where this application or proceeding is assigned is (571) 273-8300.
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/NATALIE M MOSS/ Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
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