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 ACTION
Application Status
Claim(s) 1-4 are pending in this application.
No claims have been withdrawn.
Priority
Acknowledgment is made of applicant’s claim for foreign priority under 35 U.S.C. 119 (a)-(d). The certified copy has been filed in parent Application No. TW112146913, filed on 12/01/2023.
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.
Claim 1 recites the limitation "as listed in the specification" in claim 1c, line 8. There is insufficient antecedent basis for this limitation in the claim. Claims may not use the specification as a glossary and must stand on their own. The specification may be used to define terms as to the meaning of a phrase or term but may not be used to refer back to as the specification is not a part of the claim.
Appropriate action is required.
Claim 1 recites the limitation "concentration is in the range of" in claim 1 c, line 9-10. There is insufficient antecedent basis for this limitation in the claim. It is not clear which concentration applicant is referring to. Applicant states that the keratin hydrolysis solution contain “at least 253 peptides”, but does not state which peptide concentration of the 253 peptides it is referring to.
Appropriate action is required.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
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Claim(s) 2 is rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by WO 03006531 A1, SCHROOYEN PETER MARCHEL, MYRIAM OBERTUR RADULF, FIT, 07/12/2002,(Examiner cited) hereafter regarded as Schrooyen.
In the instant case, applicants’ claim(s) 2 are directed to the method of using a keratin hydrolysis peptide solution by applying the KHP solution to asparagus bean plants at roughly 2 weeks after germination.
Regarding claim 2, Schrooyen teaches that there are some non-limiting uses of the keratins of the invention include: in the preparation thereof; use as or in formulations such as controlled release systems, e.g. for active substances such as; agrochemicals such as herbicides, pesticides or other biocides; dispersions or other multi-phasic aqueous systems; [p 16, line 17-23].
Schrooyen’s use of the term “herbicides, pesticides, or other biocides” implicitly refers to use of keratin peptides as agents against bacteria, viruses and fungus; or better termed as a fungicide for use in agriculture. It is anticipated by Schrooyen, that a hydrolyzed keratin solution would be used on asparagus bean plant to deter the fungus Fusarium and minimize wilt of the plant.
Therefore, applicant’s claim(s) 2 is anticipated by Schrooyen.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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.
Claim(s) 1 is rejected under 35 U.S.C. 103 as being unpatentable over Nurdiawati, Anissa, et al. “Liquid Feather Protein Hydrolysate as a Potential Fertilizer to Increase Growth and Yield of Patchouli.” International Journal of Recycling of Organic Waste in Agriculture, vol. 8, no. 3, September 2019, p. 221, https://doi.org/10.1007/s40093-019-0245-y (Year: 2019) (Examiner cited) , hereafter regarded as Anissa, et al., in view of evidentiary reference Silva, Tiago H., et al. “Keratin: Dissolution, Extraction and Biomedical Application.” Biomaterials Science [England], vol. 5, no. 9, August 2017, pp. 1699–735, https://doi.org/10.1039/c7bm00411g., (Examiner cited), hereafter regarded as Silva, et al. and Wan, Min-Yuan, et al. “Identification and Characterization of a Novel Antioxidant Peptide from Feather Keratin Hydrolysate. Biotechnology Letters” [Dordrecht], vol. 38, no. 4, April 2016, pp. 643–49, https://doi.org/10.1007/s10529-015-2016-9 (Year: 2016), (Examiner cited) hereafter regarded as Wan, et al.
In the instant case, applicant’s claim(s) 1 is directed to “a method of using a keratin hydrolysis peptide (KHP) solution to control and remedy the fusarium wilting”. The applicant discloses steps of preparing the KHP solution by mixing 50 kg of feathers whose water content is 50% water and 40 kg of water (biomass: water = 1:3 ) into a sealed container and hydrolyze the mixture by setting a temperature of 185°C with a pressure of 12 kg/cm2 and keeping those conditions for an 80-minute duration. The applicant states that to confirm the KHP solution having at least 253 peptides with molecular masses of between 0.5 kDa and 4 kDa by use of mass spectrometer and a concentration of 2.0 x 105 to approximately 4.5 x 105 ppm (parts per million). The applicant discloses the final step within claim(s) 1 is applying that KHP solution to soil which contains asparagus bean plant.
Regarding claim 1, Anissa, et al., teaches that [page 222, col. 1. paragraph 2-3-4] Thermochemical processing of a keratin feather solution has several advantages relative to biochemical processing, including faster reaction rates and robustness to eliminate possible pathogen microorganism. Among thermochemical methods, hydrothermal treatment (HTT) has been widely known to convert waste materials into fuels, fertilizers, biomaterials, and chemicals. The HTT is thermal conversion process in water under an autogenous pressure and relatively moderate temperatures (150–350 °C) that involves decarboxylation, hydrolysis, condensation, and dehydration reactions and has been widely investigated.
Regarding claim 1, Anissa, et al. further teaches that [p. 223, col. 2, paragraph 1 and Fig. 1] in the pilot-scale productions, the reactor was run with 10 kg of feathers and 30 kg of water (biomass:water ratio = 1:3). HTT was conducted at two different operating conditions (160 °C, 0.6 MPa and 180 °C, 0.9 MPa) to produce liquid products with varying concentrations of nutrient. The HTT-160 liquid product was applied to the mung bean, while the HTT-180 liquid product was applied to patchouli, MPa is megapascals, which is equal to 10.1972 kg/cm2.
Anissa, et al., does not teach “hydrolyzing the mixture by setting a temperature of 185°C with a pressure of 12 kg/cm2 for a duration of 80-minutes;”.
However, Silva, et al., teaches that in a pioneering process a (1 : 3 solid–liquid ratio) was treated with saturated steam at 220 °C for 10 min, and used a blow valve where the pressure was
released and a dark yellow slurry was recovered. That the dissolution and pepsin digestibility of the keratin samples obtained from SFE (steam flash explosion) or HT (heat treatment) [Fig 8] increase with the increase of the reaction pressure. A maximum dissolution of 70% was found at the highest tested pressure of 2 MPa and reports that the pepsin digestibility of 93.2% of a keratin product that was obtained from feathers through SFE under a pressure of 2 MPa, [p 1712, col 1, par 1 and col 2, par 1].
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Fig. 8 Major reactions that occur during the heat treatment of the keratin fiber.
Applicant’s pressure of 12 kg/cm2 or 1.79 MPa (megapascals) and due to the fact that Anissa, et al., used a temperature of 160°C, 0.6 MPa and 180°C, 0.9 MPa, respectively, and that Silva, et al., discusses that keratin samples, obtained from the same process, increased with increased pressure.
However, Assani, et al., does not teach the step of using a mass spectrometer to confirm the combination of peptides in the solution to contain at least 253 peptides as listed in the specification where their molecular masses are between 500 and 4,000 Daltons, and the concentration is in the range of 2.0 x105 ~ 4.5 x105 ppm.
Applicant’s claim 1, states that to verify the keratin peptides and present amino acids identified in the sequence list, applicant uses “a mass spectrometer to confirm the combination of peptides in the solution to contain at least 253 peptides as listed in the specification where their molecular masses are between 500 and 4,000 Daltons, and the concentration is in the range of 2.0 x105 ~ 4.5 x105 ppm”.
While Assani, et al. uses [page 224, col. 1, p. 1) a TOC-L/TN analyzer for total organic carbon (TOC) and total N (nitrogen) of the liquid feather protein hydrolysate (FPH). The ultimate composition (C, H, N, and ash) of solid raw materials were analyzed using Vario Micro Cube Elemental Analyzer. Micronutrients’ content was determined using ICPE-9000 (Inductively Coupled Plasma Emission Spectrometer). Chemical decomposition using a mixture of concentrated acids is required prior to ICPE analysis to dissolve the matrices of organic as well as inorganic samples. Anissa, et al. does not teach use of mass spectrometer to confirm a combination of at least 253 peptides contained within the keratin hydrolyzed solution.
However, regarding claim 1, Wan, et al. teaches that after RP-FPLC purification, peptide samples were subjected to matrix-assisted laser desorption/ionization time-of-flight/TOF tandem mass spectroscopy (MS/MS) using an ABI 4800 Plus MALDI TOF/TOF system at the Shanghai Boyuan Institute of Biotechnology; [page 664, col. 2, p. 3].
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Fig 2 [page 647]. Shows a mass spectrometry mass to charge ratio of ions (fragments of peptides) formed by peptides, ranging from as low as 20 to as high as 300. The higher the intensity the more of those peptide fragments present. Therefore, Wan, et al. teaches that there is at least 253 peptides (upwards of 860 peptide fragments).
Regarding claim 1, Wan, et al. also teaches that the Data were gathered in centroid mode covering the mass/charge (m/z) and used to search the NCBInr database on the Mascot Server to identify the peptides’ amino acid sequences; [page 664, col. 2, p. 3].
Therefore, for the reasons described above by Anassi, et al. and in lieu of Wan, et al., it would be obvious to one skilled in the art to use mass spectrometry to find fragmentation which would lead to a minimum of 253 peptides averaging a molecular weight of 0.5 kDa to 4 kDa in a concentration of 2 – 4.5 x 105 ppm.
Claims 3-4 are rejected under 35 U.S.C. 103 as being unpatentable over US 5171682 A, Shih, Jason and Williams, C. Michael, published 12/15/1992, (Examiner cited), hereafter regarded as Shih, et al. and further in view of MPEP 2144.05(II)(A).
Applicant’s claim(s) 3-4 are directed to dilution factors or ratios “wherein the solution is diluted with water by volume at the ratio of 1: 100 – 1,000” and “wherein the diluted solution is diluted with water by volume at the ratio of 1: 250 – 500”, respectively.
Shih, et al., teaches that the purified enzyme (keratin solution) can be provided in aqueous solutions having concentrations ranging from 0.05 to 5 mg/ml, and more particularly having concentrations from 0.1 to 1 mg/ml, but various concentrations can be prepared by concentration and dilution procedures known to those skilled in the art of protein purification.
In view of the teachings of Shih, et al. it would have been prima facie obvious for
one of ordinary skill in the art before the effective filing date of the instant application to modify the teachings of Shih et al. by manipulating the concentration and ratio of diluted keratin hydrolyzed solution and arrive at the dilution ratios of each of these claim(s) 3-4, by routine optimization. As per MPEP 2144.05(II)(A) generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. Based on the teachings of Shih, et al., one of ordinary skill in the art would have recognized the importance of a diluted ratio of keratin to water solution and would have been motivated to change their concentrations as part of the keratin hydrolyzed solution. There would have been a reasonable expectation of success since the reference of Shih, et al. already provides all the information to make a keratin hydrolyzed solution with the explanation of various concentrations and dilutions for a desired effect.
Therefore, claim(s) 3-4 would have been prima facie obvious over the reference of
Shih, et al. and as described above, applicants’ claim(s) 3-4 are unpatentable over Shih, et al. and as a matter of routine optimization in the pertinent art and are rejected.
Conclusion
Claims 1-4 are rejected in this application.
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/JOSEPH RICCI MATTHEWS/Examiner, Art Unit 1656
/MANJUNATH N RAO/Supervisory Patent Examiner, Art Unit 1656
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