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 .
Priority
This application claims benefit of priority to Republic of Korea Application No. KR10-2020-0156903 filed on 11/20/2020. This application is also a 371 of PCT/KR2021/017074 filed on 11/19/2021. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. However, an English translation of the foreign patent documents was not provided. Therefore, for the purposes of applying prior art, the effective filing date of the claimed invention is the filing date of the PCT, 11/19/2021.
Information Disclosure Statement
The Information Disclosure Statement filed 11/13/2025 has been acknowledged and considered.
Amendment and Claim Status
In the reply filed 02/19/2026, Applicant amended claims 1-2, 4, 6 and 10, canceled claim 8 and added new claim 12. Claims 1-5 remain withdrawn.
Claims 1-7 and 9-12 are currently pending.
Claims 1-5 are withdrawn by the Examiner as they are not encompassed by the elected group.
Claims 6-7 and 9-12 are under examination.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(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.
Claims 6-7 and 9-12 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Eikmanns et al. (US 20020065403 A1, 05/30/2002) (Of Record) as evidenced by Gokarn et al. (US 20030087381 A1, 05/08/2003) (Of Record).
Regarding claims 6-11, Eikmanns et al. disclose a process for the fermentative preparation of L-amino acids utilizing Coryneform bacteria, which already produce L-amino acids as specifically stated by Eikmanns et al., wherein the nucleotide sequence which codes for the PCK (phosphoenolpyruvate carboxykinase) gene are attenuated, and therefore expressed at a low level (See entire document, More specifically, Paragraph [0033]).
The PCK gene codes for the enzyme phosphoenol pyruvate carboxykinase (PEP carboxykinase) in C. glutamicum (Paragraph [0059]). Eikmanns et al. further disclose SEQ ID NO. 2, a polypeptide with PEP carboxykinase activity (Paragraph [0032]), more specifically, an amino acid sequence of the PCK gene from C. glutamicum (Paragraph [0067]). As the gene is from C. glutamicum and the bacterial cell used is C. glutamicum, the PCK gene represented by SEQ ID NO. 2 of Eikmanns et al. reads on an intrinsic protein. Additionally, Eikmanns et al. disclose:
A process for the fermentative preparation of L-amino acids, wherein bacteria in which
a) the polynucleotide as claimed in claim 1 is attenuated or the activity of the polypeptide for which the polynucleotide mentioned codes is reduced;
b) the desired product is concentrated in the medium or in the cells of the bacteria and;
c) the product is isolated (Claim 11 of Eikmanns et al.).
Eikmanns et al. further disclose in a specific example, Example 6, that the concentration of the lysine secreted into the medium was determined (Paragraph [0108]). The amino acid concentration was then determined by means of high pressure liquid chromatography (Paragraph [0109]). While Eikmanns et al. only disclose the concentration of lysine was determined, it appears, absent evidence to the contrary, all amino acids produced by the C. glutamicum would be secreted into the medium and recovered when the lysine concentration in the medium was determined.
The polynucleotide which codes for a polypeptide of claim 1 comprises SEQ ID NO.2 (Claim 1 of Eikmanns et al.). SEQ ID NO. 2 of Eikmanns et al. shares 100% sequence identity to instant SEQ ID NO. 1. Sequence alignment provided below.
PNG
media_image1.png
1000
652
media_image1.png
Greyscale
It is noted, as discussed above, Eikmanns et al. disclose Coryneform bacteria naturally produce L-amino acids (Paragraph [0033]). It is further noted the instant Specification indicates Corynebacterium glutamicum ATCC13032 is a wild type strain (Page 28, Example 2, First Paragraph) and goes on to disclose strain ATCC13032, with no changes, produced 0.89 g/L of L-glutamine (Page 30, Table 30). Therefore, it appears, absent evidence to the contrary, Corynebacterium glutamicum naturally produces at least some L-glutamine.
Additionally, Gokarn et al. disclose metabolically engineered organisms for enhanced production of oxaloacetate-derived biochemicals (Title), wherein glutamine is one of the oxaloacetate-derived biochemicals which can be produced (See entire document, More specifically, Paragraph [0061]). Gokarn et al. further disclose the metabolically engineered cells can be engineered to reduce or eliminate the production of PEP carboxykinase, which catalyzes the formation of PEP from oxaloacetate, wherein preventing or reducing the expression of a functional PEP carboxykinase will result in more carbon shunted to oxaloacetate and the amino acids biosynthesized therefrom (Paragraph [0044]).
Thus, it appears, absent evidence to the contrary, reducing or eliminating the production of PEP carboxykinase in the C. glutamicum cell being fermented in Eikmanns et al. would naturally and inherently result in more carbon being shunted to oxaloacetate and in turn the production of amino acids, including glutamine, as evidenced by Gokarn et al.
Therefore, Eikmanns et al. anticipate instants claim 6 and 10-12 insofar as disclosing a fermentative process, reading on culturing, for producing L-amino acids in C. glutamicum, which naturally produces L-glutamine, wherein the native PCK gene that shares 100% sequence identity to instant SEQ ID NO. 1, which has phosphoenolpyruvate carboxykinase activity, is attenuated and expressed at low levels. Eikmanns et al. anticipate instant claim 7 as they disclose the product is isolated, reading on recovered, from the medium at the end of the fermentative process. Eikmanns et al. anticipate instant claim 9 insofar as disclosing the PCK was from C. glutamicum. Thus, Eikmanns et al. anticipate the instant invention.
Regarding the new limitations to instant claim 6 and new claim 12, Eikmanns et al. do not explicitly disclose the microorganism has L-glutamine production ability increase by 5% or more compared to a wild type strain in which PEP carboxykinase activity is not weakened.
However, it is noted this limitation does not require the microorganism to produce 5% more compared to a wild type strain, the limitation simply requires the ability to produce 5% more. Even so, Eikmanns et al. disclose the production of lysine in C. glutamicum where one strain has a PEP carboxykinase gene deleted and the other strain is the wild type (Paragraph [0107]-[0108]). The C. glutamicum strain with the PEP carboxykinase gene deleted produced 65 mM of L-lysine while the wild type strain produced 54 mM of L-lysine (Paragraph [0109] and Table 3).
Thus, it would be expected, absent evidence to the contrary, that the microorganism of Eikmanns et al. would naturally and inherently have the ability to produce 5% more glutamine than a wild type strain in which PEP carboxykinase activity is not weakened as it was shown to increase the production of lysine greater than 5% compared to the wild type strain and Eikmanns et al. specifically state C. glutamicum strain can produce multiple L-amino acids (Paragraph [0033]). It would be expected glutamine would be one of those amino acids because, as disclosed above, C. glutamicum naturally produces glutamine, and Gokarn et al. disclose metabolically engineered cells can be engineered to reduce or eliminate the production of PEP carboxykinase, which catalyzes the formation of PEP from oxaloacetate, wherein preventing or reducing the expression of a functional PEP carboxykinase will result in more carbon shunted to oxaloacetate and the amino acids biosynthesized therefrom (Paragraph [0044]), including glutamine. Therefore, absent evidence to the contrary, the microorganism of Eikmanns et al. would naturally and inherently have the ability to produce 5% more glutamine than a wild type strain in which PEP carboxykinase activity is not weakened.
USC § 102 – Response to Arguments
Applicant's arguments filed 02/19/2026 have been fully considered but they are not persuasive.
Applicant argued on Page 4 that Eikmanns fails to disclose each and every feature of amended claim 6 because Eikmanns fails to disclose the microorganism has L-glutamine production ability increased by 5% or more compared to a wild type strain.
The Examiner respectfully disagrees. It is noted this a new limitation and is addressed in the modified rejection set forth above as necessitated by amendment.
Applicant further argued on Pages 4-5 that Gokarn fails to show that an increase in oxaloacetate necessarily results in production of L-glutamine.
It is the Examiner’s position that Gokarn does show that an increase in oxaloacetate necessarily results in production of L-glutamine for the reasons stated in the rejection set forth above.
Applicant additionally argued Petersen, a reference provided by Applicant, demonstrates that an increase in oxaloacetate does not necessarily lead to glutamine production.
The Examiner respectfully disagrees. Applicant specifically states Pederson demonstrates that the increase in oxaloacetate does not necessarily lead to glutamine production. However, it is unclear how Peterson is intended to support the conclusion that an increase in oxaloacetate would not necessarily lead to glutamine production when Pederson does not mention glutamine at all. Pederson discusses glutamate, but not glutamine. The instant claims are directed to glutamine. Thus, Applicant’s arguments are not persuasive.
Conclusion
Claims 6-7 and 9-12 are rejected.
No claims are allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. 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 nonprovisional extension fee (37 CFR 1.17(a)) 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 mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ASHLEY T WHITE whose telephone number is (571)272-0683. The examiner can normally be reached Monday - Friday 8:30 - 5:00 EST.
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, Sharmila Landau can be reached at (571)272-0614. 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.
/A.T.W./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653