DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after December 09, 2023, is being examined under the first inventor to file provisions of the AIA .
Status of the Application
Receipt is acknowledged of Applicants’ claimed invention filed on 12/09/2023 in the matter of Application N° 18/534,638. Said documents are entered on the record. The Examiner further acknowledges the following:
Thus, claims 1-8 represent all claims currently under consideration.
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.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 3, 4, 7, and 8 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 3, 4, 7, and 8, are unclear in reciting “ratio of 1:125-1000” and 1:300-500 in claims 3, 4, 7, and 8. It is unclear if this ratio range is 1:125 to 1000:1 or 1:300 to 500:1. Since each interpretation has a different scope, the metes and bounds of the claims cannot be determined and the claims are indefinite.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 1-8 are rejected under 35 U.S.C. 103 as being unpatentable over Juarez Molina et al. (WO2023/001946) in view of Nurdiawati et al., “characterization of potential liquid fertilizers obtained by hydrothermal treatment of chicken feathers,” environmental progress & sustainable energy, 37:375-382 (2018), and further in view of Boselli et al., “protein Hydrolysates effects on grapevine (vitis vinifera L., cv. Corvina) performance and water stress tolerance,” Scientia Horticulturae 258 (2019) 108784), and Zhang et al. (2015), “Steam Flash Explosion Assisted Dissolution of Keratin from Feathers,” ACS Sustainable Chemistry & Engineering, and Coward-Kelly et al., Bioresource Technology 97 (2006) 1337-1343, and Antioxidant peptides generated from chicken feet protein hydrolysates Burcu Ozturk-Kerimoglu,a et al., and Wei et al. (WO2016/054310), Yongsheng et al. (CN114394866A), and Aihara et al. (EP1731528A1), and Kroh et al. (US10968145B2), and Hong et al. (CN103058749B).
Regarding claim1, Juarez Molina et al. teach a process for producing a keratin hydrolysate comprising peptides and/or amino acids from a keratin-containing starting material. Juarez Molina et al. recognize feathers as keratin containing material and specifically teach that bird feathers have a high keratin content. Juarez Molina et al. further teach mixing the keratin-containing material with water and subjecting the material to elevated temperature and pressure to disrupt the keratin fibrous structure and facilitate subsequent hydrolysis.
Juarez Molina et al. further teaches that the resulting keratin hydrolysate comprises peptides having molecular weights between about 150 and 10,000 Daltons (See page 3, lines 29-31), which encompasses the instantly claimed molecular-weight range of 500 to 4,000 Daltons.
Juarez Molina et al. additionally teach that the resulting liquid mixture comprising peptides and/or amino acids may be used as an agricultural biostimulant to improve and/or stimulate plant development and may be applied to plants at different stages of development by methods including foliar application or leaf spraying.
Juarez Molina et al., however, do not expressly teach hydrolyzing a feather/water mixture at the instantly claimed temperature of 185°C, nor do Juarez Molina et al. specifically exemplify the claimed feather/water proportions.
Nurdiawati et al. cure these deficiencies in part.
Nurdiawati et al. teach the hydrothermal treatment of chicken feathers with water to produce a soluble hydrolyzed feather product suitable for use as a liquid fertilizer. Nurdiawati et al. investigate hydrothermal treatment temperatures ranging from about 140°C to 200°C (See Abstract). Thus, the instantly claimed hydrolysis temperature of 185°C lies within the temperature range expressly disclosed by Nurdiawati et al.
Nurdiawati et al. further exemplify hydrothermal treatment of chicken feathers at 180°C for 30 minutes using a feather-to-water ratio of 1:5, which resulted in solubilization of as much as approximately 83% of the chicken-feather protein. The resulting liquid contained nitrogen and amino acids and was identified as having utility as a liquid nitrogen fertilizer (See Abstract).
It would have been prima facie obvious to one of ordinary skill in the art, prior to the effective filing date of the claimed invention, to modify the keratin-hydrolysis process of Juarez Molina et al. by employing the hydrothermal feather-processing conditions taught by Nurdiawati et al., including processing feathers in water at a temperature within the disclosed range of 140-200°C, because Nurdiawati et al. expressly teach that such conditions effectively solubilize feather protein and provide a soluble hydrolyzed feather product suitable for agricultural use.
One of ordinary skill in the art would have been motivated to make such a modification because both references concern conversion of keratin rich materials into soluble products useful in agricultural applications, and Nurdiawati et al. specifically demonstrate that hydrothermal processing of feathers in water at elevated temperatures effectively solubilizes feather protein. The skilled artisan would have had a reasonable expectation that employing the hydrothermal conditions of Nurdiawati et al. in the keratin-conversion process of Juarez Molina et al. would successfully produce a soluble feather-derived hydrolysate suitable for agricultural application.
The selection of 185°C would have been prima facie obvious because that temperature lies within Nurdiawati et al’s expressly disclosed 140-200°C hydrothermal-treatment range. Moreover, Nurdiawati et al. demonstrate successful feather-protein solubilization at 180°C, only 5°C below the instantly claimed temperature.
Juarez Molina et al. in view of Nurdiawati et al., however, do not specifically teach applying the resulting keratin hydrolysis peptide solution to grape leaves during the grape plant’s fruit expansion for improving production yield.
Boselli et al. cure this deficiency.
Boselli et al. teach treating grapevines (Vitis vinifera L., cv. Corvina) with protein hydrolysates for improving grapevine performance, yield, and fruit quality. Boselli et al. applied protein hydrolysates to grapevines by spraying the compositions every ten days for three treatments from fruit-set to bunch closure, thereby teaching foliar treatment of grapevines with protein hydrolysates during grapefruit development.
Boselli et al. further demonstrate that protein hydrolysate treatment increased grape production yield. Particularly, treatment with soybean and casein protein hydrolysates at 6.4 g/L produced yields of approximately 5.57 and 5.39 kg/vine, respectively, compared with approximately 4.25 kg/vine for the untreated control, representing increases in yield of approximately 24% and 21%.
It would have been prim facie obvious to one of ordinary skill in the art, prior to the instant effective filing date of the claimed invention, to apply the keratin-derived peptide hydrolysate of Juarez Molina et al., as modified by the feather hydrothermal-processing teachings of Nurdiawati et al., to the leaf surfaces of grape plants during fruit development, as taught by Boselli et al., for the purpose of improving grape production yield.
One of ordinary skills in the art would have been motivated to do so because Juarez Molina et al. teach that keratin-derived peptide -containing liquid mixtures are useful as agricultural biostimulants and may be applied by foliar treatment; Nurdiawati et al. establish that hydrothermally processed chicken feathers provide soluble hydrolyzed products suitable for fertilizer applications; and Boselli et al. specifically demonstrate that spraying protein hydrolysates onto grapevines during fruit development improves grapevine yield and quality. One of ordinary skill in the art would have had a reasonable expectation that application of the feather-derived peptide hydrolysate to grapevines during fruit development would similarly provide beneficial effects on grape production.
Regarding the remaining processing parameters, Nurdiawati et al. teach that hydrothermal treatment conditions, including temperature, treatment time, and feather-to-water ratio, are process variables affecting feather-protein solubilization. Nurdiawati et al. exemplify treatment at 180°C for 30 minutes with a feather-to-water ratio 1:5 and investigate temperatures throughout the range of 140-200°C. Thus, Nurdiawati et al. provide a factual basis demonstrating that these hydrothermal-processing parameters were known variables associated with conversion of feathers into soluble hydrolyzed products.
However, the cited references do not appear to expressly disclose the complete claimed combination of 185°C, 12 kg/cm2, and 80 minutes, nor have the references presently been identified as expressly teaching confirmation by mass spectrometry of at least 253 particular peptides, each having 5-30 amino acids, or concentration of the resulting solution to 300,000-450,000 ppm. These limitations require separate consideration.
With regard to the instantly claimed pressure of 12 kg/cm2 and hydrolysis duration of 80 minutes, the prior art further establishes that pressure and treatment time were recognized result-effective variables in the processing and hydrolysis of feather keratin.
For example, Zhang et al. teach steam-flash explosion treatment of feathers at different steam pressures ranging from 1.4 to 2.0 MPa and treatment times ranging from 0.5 to 5 minutes and expressly evaluate the effects of pressure and treatment time on feather extraction and keratin yield. Zhang et al. demonstrate that varying steam pressure affects the extent of feather extraction and keratin recovery, thereby establishing that pressure was a known process variable affecting keratin conversion (See Abstract).
Moreover, Nurdiawati et al. teach hydrothermal processing of feathers at approximately 180°C and 9.2kg/cm2, whereas Zhang et al. investigate pressures beginning at approximately 1.4 MPa (about 14.3 kg/cm2). Thus, the instantly claimed pressure of 12 kg/cm2 falls between pressure conditions known in the art to be useful for thermal processing of feather keratin.
Coward-Kelly et al. further establish that reaction time is a result-effective variable in feather-keratin hydrolysis. Coward-Kelly et al. expressly investigate the effects of treatment conditions, including temperature and reaction time, on hydrolysis of chicken-feather keratin. Coward-Kelly et al. disclose that at 150°C approximately 80% of feather keratin was solubilized within 25 minutes, whereas approximately 300 minutes were required at 100°C to obtain a comparable degree of solubilization. Coward-Kelly et al. further report that approximately 95% of feather keratin was digested after three hours at 150°C (See Abstract).
The prior art establishes that temperature, pressure, and reaction time were known process parameters affecting the extent of feather-keratin disruption, solubilization, and hydrolysis. It therefore would have been within the ordinary skill in the art to optimize these known process variables to obtain a desired extent of feather hydrolysis. Selection of 185°C, 12 kg/cm2, and 80 minutes would have represented optimization of known result effective process variables, particularly where the claimed temperature falls within Nurdiawati et al.’s disclosed 140-200°C range and the claimed pressure and treatment time fall within or between conditions known in the art for processing feather keratin.
With regard to the limitation requiring use of a mass spectrometer to confirm the peptide composition of the hydrolysate, Ozturk-Kerimoglu et al. provide evidence that mass spectrometric analysis was a known technique for characterizing complex peptide mixtures obtained by hydrolysis of poultry-derived proteins. Ozturk-Kerimoglu et al. subjected poultry protein hydrolysates to nano-liquid chromatography coupled with tandem mass spectrometry (nLC-MS/MS) and identified more than 230 individual peptide sequences in the resulting hydrolysate (See Abstract).
Ozturk-Kerimoglu et al. further disclose identified peptides having molecular weights of approximately 700.8 to 1092.3 Daltons and peptide lengths of approximately 7-12 amino acid residues, which fall within the instantly claimed ranges of 500-4,000 Daltons and 5-30 amino acids (See page 7212).
It would have been obvious to one of ordinary skill in the art, prior to the instant effective filing date of the claim invention to characterize the peptide-containing feather hydrolysate produced according to the teachings of the cited references using a known mass-spectrometric peptide-identification technique, such as the technique taught by Ozturk-Kerimoglu et al., for the predictable purpose of determing the number, identity, molecular mass, and amino-acid length of peptides present in the hydrolysate.
The Examiner further notes that the recited presence of at least 253 peptides does not necessarily impart patentable distinction to the claimed method where the peptides are the resulting products of processing the same keratin-containing starting material, i.e., feathers, according to the same or substantially similar hydrolysis conditions taught or suggested by the prior art.
In particular, the cited prior art teaches the hydrolysis of feathers under temperature, pressure, and reaction-time conditions that are the same as, overlap with, or would have been obvious to optimize to arrive at the presently claimed processing conditions. Where the same starting material is subjected to the same or substantially similar processing conditions, one of ordinary skill in the art would reasonably expect the resulting hydrolysate to contain the same or substantially similar population of keratin-derived peptides.
Once the prior-art process is modified to employ the instantly claimed or otherwise obvious hydrolysis conditions, the resulting peptide profile, including the number, molecular masses, and amino-acid lengths of the peptides, would reasonably be expected to result from the hydrolysis process rather than constitute a separately manipulated process limitation.
Moreover, the recited step of using a mass spectrometer to confirm the presence of the peptide does not itself cause formation of the peptides but instead constitutes an analytical step for identifying or characterizing peptides already present in the resulting hydrolysate. The prior art further establishes that mass spectrometry was a known analytical technique for identifying and characterizing peptides in protein hydrolysates.
Thus, absent persuasive evidence demonstrating that the recited population of at least 253 peptides results from a materially different process or possesses an unexpected property relative to the peptide population produced by the same or substantially similar prior-art feather-hydrolysis process, the recited peptide characterization does not overcome the prima facie case of obviousness.
Wei et al. teach methods of applying peptide containing compositions to a broad variety of plants for promoting beneficial plant responses, including improved plant growth and increased yield. Wei et al. further disclose that the peptide compositions may be applied to numerous plant species, thereby demonstrating that the beneficial effects of peptide treatment are not limited to a single plant species.
The teachings of Wei et al. provide further evidence that, prior to the effective filing date of the instant application, it was known in the art to apply peptide-containing compositions to a wide variety of plants for the purpose of improving plant growth and/or production yield. Thus, one of ordinary skill in the art would have had reason to apply a peptide-containing keratin hydrolysate, such as that taught by Juarez Molina et al. and Nurdiawati et al., to a selected agricultural crop with a reasonable expectation of obtaining a beneficial plant-growth or yield response.
Regarding claim 2, The combined references do not expressly teach applying the peptide-containing solution to the surface of grape leaves specifically during the fruit thinning stage.
However, Boselli et al. teach foliar application of protein hydrolysates to grapevines during the fruit-development period. Specifically, Boselli et al. teach spraying protein hydrolysates onto grapevines every ten days for three applications from fruit set to bunch closure, and further demonstrate that such treatment improves grapevine performance and production yield (See page 5).
It would have been obvious to one of ordinary skill in the art, prior to the instant effective filing date of the invention to apply the peptide-containing solution to grape leaves during the fruit thinning stage, because Boselli et al. teach repeated foliar application of protein hydrolysates during grape fruit development as a parameter available for selection by the skilled artisan.
Selection of the fruit thinning stage as the particular time for foliar application would have involved no more than selecting an appropriate application time within the known fruit development treatment period taught by Boselli et al., with a reasonable expectation of obtaining the known beneficial effects of protein-hydrolysate treatment on grapevine performance and yield. No criticality or unexpected result attributable specifically to application at the fruit thinning stage has been established.
Regarding claim 3, Yongsheng et al. teaches an amino acid/polypeptide-containing liquid fertilizer intended for agricultural application and expressly teaches dilution of the liquid fertilizer with water prior to foliar spraying. In particular, Yongsheng et al. teaches mixing the amino acid liquid fertilizer with water at a ratio of 1:400-500 fertilizer to water, including an expressly exemplified ratio of 1:500, followed by spraying onto the leaf surfaces of crops during stages of plant and fruit development (See claim 10).
Expressed in the same orientation as instant claim 3, the disclosed 1:500 fertilizer-to-water ratio corresponds to approximately 500 parts water to 1 part fertilizer solution, which falls squarely within the instantly claimed range of 125-1,000 parts water to 1 part solution.
It would have been obvious to one of ordinary skill in the art, prior to the instant effective filing date of the invention to dilute the peptide-containing solution of Juarez Molina et al., as modified by Nurdiawati et al. and applied to grape plants according to Wei et al. and Boselli et al., using a water dilution ratio such as that taught by Yongsheng et al., prior to foliar application. One of ordinary skill in the art would have been motivated to do so because Yongsheng et al. expressly teaches that amino-acid-and polypeptide-containing agricultural liquid compositions are diluted with water at such ratios for effective foliar application to plant leaf surfaces.
Selection of a dilution ratio within the instantly claimed range would have been obvious because the prior art expressly teaches a 500:1 water-to-solution ratio, which lies within the claimed 125-1,000:1 range, with a reasonable expectation that the diluted peptide-containing composition would remain suitable for foliar application.
Regarding claim 4, the combined references do not expressly teach diluting the keratin hydrolysis peptide solution with water at the instantly claimed volume ratio of 300-500 parts water to 1-part soluition.
However, Yongsheng et al. teaches an amino-acid-and polypeptide-containing liquid fertilizer for agricultural application and expressly teaches dilution of the liquid fertilizer with water prior to foliar spraying. Yongsheng et al. teaches diluting the amino acid liquid fertilizer with water at a ratio of 1:400-500 fertilizer to water, including an expressly disclosed ratio of 1:500, followed by spraying the diluted composition onto plant leaf surfaces (See claim 10).
Expressed in the same orientation as instant claim 4, the disclosed fertilizer-to-water ratios correspond to approximately 400-500 parts water to 1 part fertilizer solution, which fall within the instantly claimed range of 300-500 parts water to 1 part solution.
It would have been obvious to one of ordinary skill in the art, prior to the instant effective filing date at the time of the invention to dilute the peptide-containing solution of Juarez Molina et al., as modified by Nurdiawati et al. and applied to plants according to Wei et al. and Boselli et al., using the dilution ratios taught by Yongsheng et al. prior to foliar application. One of ordinary skills in the art would have been motivated to employ such dilution because Yongsheng et al. expressly demonstrates that amino-acid-and polypeptide-containing agricultural liquid compositions are diluted with substantial quantities of water within the instantly claimed range for effective application to plant leaf surfaces.
The instantly claimed 300-500:1 water-to-solution ratio would have been prima facie obvious because the prior art expressly teaches 400-500:1 water-to-solution ratios, which overlap the claimed range, with a reasonable expectation that the resulting diluted peptide-containing composition would remain suitable for foliar application.
Regarding claim 5, Juarez Molina et al. teach processes for producing keratin hydrolysates comprising peptides and/or amino acids from keratin-containing starting materials. Juarez Molina et al. expressly recognizes animal feathers, including bird feathers, as keratin-rich starting materials and teach conversion of keratin-containing material using water, elevated temperature and pressure, and hydrolysis to produce a liquid mixture comprising peptides and/or amino acids.
Juarez Molina et al. further teaches that the resulting hydrolysate comprises peptides having molecular weights between approximately 150 and 10,000 Daltons, which encompasses the instantly claimed range of 500-4,000 Daltons. Juarez Molina et al. additionally teaches use of the resulting peptide containing liquid mixture as an agricultural biostimulant that may be applied to plants by foliar application to improve or stimulate plant development.
Juarez Molina et al., do not expressly teach processing 70 kg of feathers having 46% water content of 180°C and 13 kg/cm2 for 40 minutes.
Nurdiawati et al. cure these deficiencies in part. Nurdiawati et al. teach hydrothermal treatment of chicken feathers in water to obtain soluble hydrolyzed feather products suitable for use as liquid fertilizer. Nurdiawati et al. investigate hydrothermal processing over approximately 140-200°C and expressly exemplify treatment at 180°C, which is identical to the temperature recited in instant claim 5.
The prior art further establishes that temperature, pressure, and reaction time were recognized process variables affecting the disruption, solubilization, and hydrolysis of feather keratin. It would have been obvious to one of ordinary skill in the art to select and optimize the pressure and duration of hydrothermal feather treatment to obtain a desired degree of keratin hydrolysis and solubilization. The claimed 180°C, 13 kg/cm2 and 40-minute treatment represents selection of known hydrothermal processing parameters for the known purpose of converting feather keratin into a soluble hydrolysate.
With regard to the claimed 70 kg quantity of feathers, the particular scale or batch quantity does not appear to alter the underlying keratin hydrolysis process. Once feathers were selected as the keratin starting material, selection of an appropriate batch quantity would have been within the ordinary skill in the art and dependent upon the desired production scale and capacity of the processing equipment.
With regard to the recitation that the feathers have a 46% water content, the prior art teaches processing feathers in the presence of water and recognizes water content as part of the hydrothermal processing system. Selection of an appropriate amount of water relative to feather material would have been a known process parameter available for adjustment to provide the desired hydrothermal reaction conditions.
With regard to the recitation that the resulting solution contains at least 253 peptides having molecular masses between 500 and 4,000 Daltons and consisting of 5-30 amino acids, Juarez Molina et al. teach production of peptide-containing hydrolysates from keratin material having a molecular-weight distribution encompassing the instantly claimed range. The Examiner further notes that the recited peptides are products resulting from hydrolysis of the feather starting material. Where the same keratin-containing starting material is subjected to the same or substantially similar hydrothermal-hydrolysis conditions, one of ordinary skill in the art would reasonably expect the resulting hydrolysate to contain the same or substantially similar population of keratin derived peptides.
The recitation of using a mass spectrometer to confirm the peptide composition constitutes an analytical characterization of the resulting hydrolysate rather than a step responsible for producing the peptides. Mass spectrometry was known in the art for identifying and characterizing peptides in protein hydrolysates, including determining peptide number, molecular mass, and amino-acid sequence or length. Thus, it would have been obvious to characterize the resulting peptide-containing hydrolysate using known mass-spectrometric analytical techniques.
The combined teachings of Juarez Molina et al. and Nurdiawati et al., however, do not specifically teach applying the resulting peptide-containing solution to grape leaf surfaces during the grape plant’s fruit expansion stage for improving production yield.
Wei et al. teach application of peptide compositions to a broad variety of plants for obtaining beneficial plant responses, including improved plant growth and production yield, thereby establishing that agricultural peptide treatments were not limited to a single plant species.
Boselli et al. further teach specifically treating grapevines with protein hydrolysates by foliar spraying during grape fruit development, including applications from fruit set to bunch closure, and demonstrate improved grapevine production yield.
It would have been obvious to one of ordinary skill in the art, prior to the instant effective filing date of the claim invention to apply the feather derived peptide hydrolysate taught by Juarez Molina et al., and Nurdiawati et al. to grape leaf surfaces during fruit development as taught by Boselli et al., with a reasonable expectation of improving grapevine performance and production yield. Wei et al. further supports the reasonable expectation that peptide-containing compositions may beneficially be applied across different agricultural plant species.
With regard to filtering and concentrating the resulting hydrolysate, filtration and concentration constitute conventional post-hydrolysis processing operations for removing residual insoluble material and obtaining a peptide-containing liquid composition of a desired concentration. The particular concentration selected would depend upon the concentration appropriate for storage and subsequent dilution/application. However, the Examiner relies upon the additional evidence of record concerning concentration of protein/peptide hydrolysates in establishing the obviousness of the instantly claimed 300,000-450,000 ppm concentration range.
Aihara et al. further teaches hydrolysis of keratin-containing raw materials, including feathers, wherein the water content of the keratin raw material is adjusted prior to hydrolysis. Aihara et al. teaches a water content range of 20-80%, preferably 25-80%, and more preferably 30-75%, each of which encompasses the instantly claimed feather water content of 46% (See paragraph 0016). Aihara et al. further exemplifies feathers having a water content of 50% (See paragraph 0029), which is close to the instantly claimed 46%.
Aihara et al. establishes that the water content of the feather starting material is a result-effective variable affecting hydrolysis. Specifically, the reference teaches that increasing the water content of the keratin raw material decreases its bulk volume, improves affinity between the raw material and solvent, and permits hydrolysis to be performed more efficiently. Aihara et al. experimentally evaluates feather water contents of 12%, 20%, 30%, 40%, 50%, 60%, 70%, and 80% and reports improved hydrolysis when the water content is 20% or greater (See paragraph 0040).
It would have been obvious to one of ordinary skill in the art, prior to the instant effective filing date of the claim invention to employ feathers having a water content of 46%, because 46% falls within the expressly disclosed and preferred water-content ranges and represents selection of a known result-effective variable for promoting efficient feather-keratin hydrolysis.
With regard to the limitation requiring the resulting hydrolysate solution to be filtered and concentrated to 300,000-450,000 ppm, the prior art establishes that concentrated protein and amino-acid hydrolysate liquids having concentrations within the instantly claimed range were known.
Kroh et al. teaches preparation of a protein hydrolysate liquid comprising free amino acids and expressly discloses that the resulting hydrolysate liquor contains about 30-35% dissolved solids. The reference further teach that such concentrated amino-acid hydrolysate compositions are useful in agricultural applications for promoting plant growth (See Description, paragraph 4).
The instantly claimed concentration of 300,000-450,000 ppm corresponds approximately to 30-45% on a mass basis. Thus, the 30-35% dissolved-solids concentration expressly disclosed by Kroh et al. falls within the instantly claimed concentration range.
Hong et al. further teaches preparation of an amino-acid liquid fertilizer by hydrolysis of animal protein, followed by filtration and concentration of the resulting hydrolysate (See Abstract). Hong et al. also recognizes 30% amino-acid liquid fertilizer as a conventional agricultural formulation and demonstrates foliar application of amino-acid liquid fertilizers for improving plant yield and quality (See Table 1, Amino Acid Liquid Fertilizer Formulation Example (Unit: Kilogram).
It would have been obvious to one of ordinary skill in the art, prior to the instant effective filing date to filter and concentrate the feather-derived peptide hydrolysate to a concentration within the instantly claimed 300,000-450,000 ppm range because the prior art teaches both concentrating protein hydrolysates after hydrolysis and using concentrated amino-acid/protein hydrolysate liquids having concentrations of about 30-35%, which fall within the claimed range.
One of ordinary skill in the art would have had a reasonable expectation that concentrating the feather-derived hydrolysate to such a level would provide a stable and practical concentrated liquid suitable for storage, handling, and subsequent dilution for agricultural applications.
Regarding claim 6, the combined references do not expressly teach applying the keratin hydrolysis peptide solution to the surface of grape leaves specifically during the grape plant’s fruit thinning stage.
However, Boselli et al. teach foliar application of protein hydrolysates to grapevines during the fruit-development period. Specifically, Boselli et al. teach spraying protein hydrolysates onto grapevines every ten days for three applications from fruit set to bunch closure. Boselli et al. further demonstrate that application of the protein hydrolysates during this fruit development period improves grapevine performance and production yield.
It would have been obvious to one of ordinary skill in the art, prior to the instant effective filing date at the time of the invention to apply the peptide-containing solution to grape leaf surfaces during the fruit thinning stage, because Boselli et al. teach repeated foliar application of protein hydrolysates during grape fruit development and thereby establish application timing during fruit development as a parameter available for selection by the skilled artisan.
Selection of the fruit thinning stage as the particular time for foliar application would have involved no more than selecting an appropriate application time within the known fruit-development treatment period taught by Boselli et al., with a reasonable expectation of obtaining the known beneficial effects of protein-hydrolysate treatment on grapevine performance and production yield. No criticality or unexpected result attributable specifically to application during the fruit thinning stage has been established.
Regarding claim 7, the combined references do not expressly teach diluting the keratin hydrolysis peptide solution with water at the instantly claimed volume ratio of 125-1,000 parts water to 1 part solution.
However, Yongsheng et al. teaches an amino-acid-and polypeptide-containing liquid fertilizer for agricultural application and expressly teaches dilution of the liquid fertilizer with water prior to foliar spraying (See Abstract). In particular, Yongsheng et al. teaches diluting the amino acid liquid fertilizer with water at a ratio of approximately 1:400-500 fertilizer to water, including an expressly disclosed ratio of 1:500, followed by spraying the diluted composition onto plant leaf surfaces (See claim 10).
Expressed in the same orientation as instant claim 7, the disclosed 1:500 fertilizer-to-water ratio corresponds to 500 parts waters to 1 part fertilizer solution, which falls within the instantly claimed range of 125-1,000 parts water to 1 part solution.
It would have been obvious to one of ordinary skill in the art, prior to the instant effective filing date of the claim invention to dilute the peptide-containing solution of claim 5 using the water-to-solution ratios taught by Yongsheng et al. prior to foliar application. One of ordinary skill in the art would have been motivated to employ such dilution because Yongsheng et al. expressly teaches dilution of amino-acid-and polypeptide-containing agricultural liquid compositions with substantial quantities of water to produce compositions suitable for application to plant leaf surfaces.
The instantly claimed 125-1,000:1 water-to-solution ratio would have been prima facie obvious because the prior art expressly teaches a 500:1 water-to-solution ratio, which falls within the claimed range, with a reasonable expectation that the resulting diluted peptide containing composition would remain suitable for foliar application and provide the known beneficial agricultural effects.
Regarding claim 8, Yongsheng et al. teaches an amino-acid and polypeptide-containing liquid fertilizer for agricultural application and expressly teaches dilution of the liquid fertilizer with water prior to foliar spraying (See Abstract). in particular, Yongsheng et al. teaches diluting the amino-acid liquid fertilizer with water at a ratio of approximately 1:400-500 fertilizer to water, followed by application of the diluted composition to plant leaf surfaces (See claim 10).
Expressed in the same orientation as instant claim 8, the disclosed fertilizer-to-water ratio corresponds to approximately 400-500 parts water to 1 part fertilizer solution, which overlaps and falls within the instantly claimed range of 300-500 parts water to 1 part solution.
It would have been obvious to one of ordinary skill in the art, prior to the instant effective filing date of the invention to dilute the peptide-containing solution of claim 5 using the water-to-solution ratios taught by Yongsheng et al. prior to foliar application. One of ordinary skills in the art would have been motivated to employ such dilution because Yongsheng et al. expressly teaches that amino acid-and polypeptide-containing agricultural liquid compositions are diluted with water within the instantly claimed range to provide compositions suitable for application to plant leaf surfaces.
The instantly claimed 300-500:1 water-to-solution ratio would have been prima facie obvious because the prior-art 400-500:1 water-to-solution range overlaps the claimed range. One of ordinary skill in the art would have had a reasonable expectation that employing a dilution within this overlapping range would provide a peptide -containing composition suitable for foliar agricultural application.
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 AlA. 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 |.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 1-8, are provisionally rejected on the grounds of nonstatutory double patenting as being unpatentable over:
claims 1, 3, and 4 of US Patent Application No. 18/902,317 (plants).
claims 1-3 of US Patent Application No.18/827,519 (cabbage).
Claims 1 and 3 of US Patent Application No.18/642,445 (asparagus).
Claims 1 3 and 4 of US Patent Application No.18/902,317 (plants).
Claim 4 of US Patent Application No.18/898,195 (rice).
Claims 1, 2, and 3 of US Patent Application No.18/827,519 (cabbage).
Claims 1-3 of US Patent Application No.18/778,049 (cabbage).
Claim 1 of US Patent Application No.18/758,198 (cotton).
Claims 1 3, 4, and 6 of US Patent Application No.18/774,885 (melon).
Claims 1, 3 5, 6, 8, and 10 of US Patent Application No.18/758,140 (tea leaves).
Claims 9-16 of US Patent Application No.18/536,211 (wheat).
Claims 4-5, and 7-9 of US Patent Application No.18/639,751 (soybean).
Claims 1- 3 of US Patent Application No.18/639,950 (soybean).
Claims 1, 2, and 4 of US Patent Application No.18/408,245 (soybean).
Claims 2, and 3 of US Patent Application No.18/409,790 (cotton).
Claims 1-5, and 7 of US Patent Application No.18/537,395 (cotton).
Claims 1-3 of US Patent Application No.18/639,950 (soybean).
Claims 1, 3, and 4 of US Patent Application No.18/642,445 (asparagus).
Claims 1, 2, 4, 5-6 and 8 of US Patent Application No.18/658,834 (lettuce).
Claims 1-6 of US Patent Application No.18/668,598 (cotton).
Claims 1-6 of US Patent Application No.18/671,848 (soybeans).
Although the conflicting claims at issue are not identical, they are not patentably distinct from each other. The respective claim sets are directed to substantially the same method of preparing and applying a keratin hydrolysis peptide (KHP) solution, with the principal distinction being the particular plant species to which the KHP solution is applied.
Most specifically, the conflicting claims recite preparing a KHP solution by combining a keratin containing starting material, such as feathers, having the same or overlapping water content with the same or overlapping amount of water in a sealed container; hydrolyzing the resulting mixture under the same, overlapping, or substantially similar temperature and pressure conditions; confirming by mass spectrometric analysis that the resulting solution contains the same 253 peptides (SEQ ID Nos: 1-253) having the same or overlapping molecular-mass and concentration ranges. diluting the resulting KHP solution with water within the same or overlapping volume-ratio ranges, including 1:125-1000 and/or 1:300-500; and applying the diluted KHP solution to a plant by substantially the same modes of administration, including soil infusion, during selected stages of plant development.
Thus, the substantive difference among the conflicting claims resides primarily in the identity of the plant being treated, for example, grape, wheat, cabbage, asparagus, lettuce, soybean, tea, or melon, rather than in the KHP composition, its method of preparation, its peptide characteristics, or the manner in which the KHP composition is administered to the plant.
The Examiner further notes that the prior art provides evidence that selection of a particular plant species from among these plant species would have been predictable rather than inventive. Specifically, Wei et al. teach that peptide compositions may be used to treat plants or plant seeds and expressly identify a broad but finite group of suitable plants, including, inter alia, alfalfa, apple, apricot, asparagus, cabbage, lettuce, cotton, melon rice, tea, wheat, and tomato (See Wei et al. paragraph 0206). Thus, Wei et al. provide evidence that peptide-based plant treatment was known to be applicable to numerous different plant species and, importantly, expressly identify the plant species recited by the conflicting claim as suitable subjects for peptide treatment.
Accordingly, one of ordinary skills in the art, presented with the KHP preparation and plant treatment method recited in one of the conflicting claim sets, would have found it obvious to employ that same method for grape plant’s rather than another expressly identified plant species, such as wheat, cabbage, asparagus, lettuce, soybean, tea, or melon. The substitution of one expressly identified and suitable plant species for another would not require a change in the underlying KHP preparation, peptide composition, or general method of treatment. Rather, it would constitute selection of a particular plant from a finite group of known plant species recognized in the art as suitable for peptide treatment, with a reasonable expectation that the peptide treatment would provide its known beneficial effect when applied to the selected plant.
Therefore, merely limiting one claim set to promoting the development and growth of grape plants, while the conflicting claims recite substantially the same KHP composition and treatment methodology for other expressly identified plant species, does not render the presently claimed method patentably distinct. The record does not establish that application of the KHP treatment to grape plants involves a different mechanism, requires materially different processing or application conditions, or produces an unexpected result sufficient to distinguish the grape plants method from the corresponding KHP treatment methods directed to the other plant species.
With respect to any differences in the numerical processing, dilution, or application parameters among the conflicting claims, the Examiner directs attention to MPEP 2144.05(I), which explains that a prima facie case of obviousness may exist where claimed ranges overlap or lie within ranges disclosed by the prior art, and may also exist where the respective ranges do not overlap but are sufficiently close such that one of ordinary skill in the art would have expected them to provide the same properties or results. Accordingly, overlapping or closely related processing and application ranges do not, without evidence or criticality or unexpected results, establish patentable distinctness between the conflicting claims.
For at least these reasons, the presently claimed method of treating grape plants with the KHP solution is not patentably distinct from the conflicting claims directed to treatment of the other identified plant species using substantially the same KHP composition, preparation process, dilution, and application methodology.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not been patented.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Kimberly Barber whose telephone number is (703) 756-5302. The examiner can normally be reached on Monday through Friday from 6:30 AM to 3:30 PM EST.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert A. Wax, can be reached at telephone number (571) 272-0623. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/KIMBERLY BARBER/Examiner, Art Unit 1615
/Robert A Wax/Supervisory Patent Examiner, Art Unit 1615
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