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. Election/Restrictions Applicant’s election without traverse of claims 1-6, 8-12, 14, 16, and 17; as well as the species elections of yeast cell (claim 1), Saccharomyces cerevisiae (claims 16-17), Tityus serrulatus (claim 4) , Chlorella virus PBCV1 (claim 8), option ( ii ) ( claim 9 ) , Pastuerella m u ltocida (claim 10) , and option ( i ) ( claim 12 ) , in the reply filed on 1/5/2026 is acknowledged. Claim s 3, 18-19, 23-30, and 32 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention or species , there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 1/5/2026. Priority This application is a 371 of PCT/EP2022/058583 ( 3/31/2022 ) which claims priority to EP21166740.7 ( 4/1/2021 ) as reflected in the filing receipt issued on 8/14/2024 . Information Disclosure Statement The information disclosure statement (IDS) filed on 9/29/2023 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the e x aminer. Drawings The drawings are objected to for the following reasons: 37 CFR 1.84(u)(1) states “View numbers must be preceded by the abbreviation “FIG.”. In the current case, the view number for Figure 1 is preceded by the word “Figure” instead of the abbreviation “FIG.”. View numbers should be updated to recite the abbreviation “FIG.”. Any changes to the drawings should also be reflected in the specification. Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance. Specification The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code ( see p. 27-28 ) . Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01. 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 1, 5-6, 11, and 16-17 are rejected under 35 U.S.C. 102 (a)(2) as being anticipated by Kang et al., WO2021077581 A1 (effective filing date 10/24/2019) , as evidenced by Jolly et al., US 9,689,010 B2 . Regarding claim 1, Kang teaches engineered yeast cells for the fermentative production of chondroitin sulfate (Kang para. 1). Kang teaches that the yeast cell expresses kfoC encoding chondroitin synthase ( Genbank accession number BAC00523.1); tuaD is a gene encoding UDP-glucose dehydrogenase ( Genbank accession number NP_391438. 1), and KfoA ( Genbank accession number BAC00525.1 ) (Kang para. 14; para. 33-36). Regarding the limitation “ wherein the recombinant yeast cell (ii) optionally further comprises ”, it is considered that the yeast cell of claim 1 is not required to comprise one or more recombinant nucleic acids encoding a polypeptide having a chondroitinase activity wherein the polypeptide having chondroitinase activity comprises a secretion signal . Therefore, Kang anticipates the engineered yeast cell of claim 1. Regarding claims 5 and 6 , the limitations “ producing chondroitin ” in claim 1 and , “ wherein the molecular weight of the chondroitin is ” in claims 5 and 6 are directed to functional limitations of the claimed cell. It is expected that any cell having the same structure as the claimed cell is capable of producing chondroitin having the claimed molecular weights. The cell of Kang has an identical structure to the cell of claim 1 (expressing chondroitin synthase, UDP-glucose dehydrogenase , and KfoA ), and produces chondroitin (Kang para. 1). While Kang does not specify the molecular weight of the produced chondroitin, it is expected that the yeast cell taught by Kang, which is identical to that of claim 1, is capable of producing chondroitin with molecular weights as set forth in claims 5 and 6. Further, as evidenced by Jolly et al., microbially-produced chondroitin is known to commonly have a molecular weight of 20,000 to 50,000 Da (20-50 kDa ) but can have molecular weights of 50,000 Da (50 kDa ) or greater (Jolly col. 1 lines 45-50; col. 4 lines 10-30). Therefore, the recombinant yeast cell of Kang is considered to be capable of producing chondroitin with a molecular weight of less than 50 kDa ( claim 5 ) or greater than 50 kDa ( claim 6 ). Regarding claim 11, Kang teaches that the nucleic acid encoding the kfoA polypeptide is derived from a bacterium, E. coli (Kang para. 14; Genbank accession number NP_391438. 1). Regarding claims 16 and 17, Kang teaches that the recombinant yeast cell is Saccharomyces cerevisiae (Kang para. 33-36). 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 . This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention. Claim 4 is rejected under 35 U.S.C. 103 as being unpatentable over Kang et al. as applied to claims 1, 5-6, 11, and 16-17 above, in view of Amorim et al., Applied microbiology and biotechnology ; 102(7):3145-58 , as evidenced by pPICZ αA SnapGene reference. Kang teaches the recombinant yeast cell of claim 1 as set forth above. Kang teaches that the recombinant yeast cell is used to produce chondroitin sulfate, which is digested with chondroitin sulfate lyase ABCI, then analyzed (Kang para. 96-97). Kang does not teach that the yeast cell comprises a recombinant nucleic acid encoding a polypeptide having a chondroitinase activity wherein the polypeptide having chondroitinase activity comprises a secretion signal , which is obtained from Tityus serrulatus ( claim 4 ) . Regarding claim 4, Amorim teaches a hyaluronidase , rTsHyal-1 (or chondroitinase , see instant specification p. 67) from Tityus serrulatus (Amorim “Abstract”). Amorim teaches that the hyaluronidase from T. serrulatus degrades chondroitin (Amorim p. 3155 para. 3). Amorim teaches heterologous expression of the T. serrulatus hyaluronidase in yeast (Amorim p. 3148 “ Laboratory-scale expression of rTsHyal-1 ”; p. 3155 para. 6). Amorim teaches that the hyaluronidase is secreted by the yeast (Amorim p. 3149 “ Heterologous expression of rTsHyal-1 ”) . Amorim teaches that of rTsHyal-1 is inserted into the plasmid pPICZ αA , which comprises an α-factor signal peptide (Amorim p. 3147 Fig. 1). The α-factor signal peptide is a secretion signal (see pPICZ αA SnapGene reference). It would have been obvious for a skilled artisan , before the effective filing date, to modify the recombinant yeast cell of Kang and additionally include a nucleic acid encoding a chondroitinase /hyaluronidase with a secretion signal as taught by Amorim. Kang teaches recombinant expression of genes involved in chondroitin production, and teaches that the chondroitin is digested with a chondroitin sulfate lyase that is added to the sample before analysis (Kang para. 96). The instant specification, p. 67, states that t he chondroitinase enzyme is a protein which is described in the art for catalyzin g the degradation of chondroitin molecules into smaller chondroitin molecules. Therefore, as Kang teaches an enzyme with chondroitinase activity is used in the production of chondroitin by the recombinant yeast (chondroitin sulfate lyase) , it would have been obvious to express a nucleic acid encoding a chondroitinase in the recombinant yeast cell, as taught by Amorim. A person of ordinary skill in the art would have been motivated to modify the yeast cell of Kang with a chondroitinase /hyaluronidase from T. serrulatus as taught by Amorim, because Kang teaches digestion of chondroitin by an enzyme in the process of using the cell to produce chondroitin, and it would be considered advantageous to directly express and produce such an enzyme by the recombinant strain rather than adding it to the chondroitin separately. As Amorim teaches that the T. serrulatus hyaluronidase degrades chondroitin, a skilled artisan would have been motivated to express this nucleic acid in a yeast cell according to Kang, with a reasonable expectation of success , given the successful recombinant expression of this hyaluronidase in yeast as taught by Amorim. Claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over Kang and Amorim as applied to claim 4 above, and further in view of Khasa et al. Yeast ; 28(3):213-26. Kang teaches the recombinant yeast cell of claim 1 as set forth above. Kang and Amorim teach a recombinant nucleic acid encoding a polypeptide having a chondroitinase activity wherein the polypeptide having chondroitinase activity comprises a secretion signal , as set forth above. These references do not teach that the chondroitinase comprises an anchoring signal, as required by claim 2 . Regarding claim 2, Khasa teaches vectors for recombinant protein secretion comprising anchoring signals ( Khasa Abstract). Khasa teaches that y east surface display technology is an attractive tool for industrial applications, ranging from whole cell biocatalysis, waste-water treatment, screening of combinatorial single-chain variable fragment ( scFv ) libraries, recombinant protein production to various diagnostic applications , and teaches that the anchoring protein system is used to secrete proteins into the culture supernatant of the yeast Pichia pastoris ( Khasa p. 214 para. 1-4). Khasa teaches that the newly developed native P. pastoris PIR protein-anchoring system would be an attractive alternative in yeast cell surface display technology and recombinant protein production ( Khasa p. 225 “Conclusion”). It would have been obvious for a skilled artisan , before the effective filing date, to modify the nucleic acid encoding a chondroitinase in the recombinant yeast cell as taught by Kang and Amorim to further include an anchoring signal. Kang and Amorim teach a chondroitinase with a secretion signal for recombinant expression and secretion by a yeast strain. Given the teachings of Khasa directed to fusion proteins with anchoring signals for recombinant protein secretion, it would have been obvious for an ordinary artisan to incorporate an anchoring signal with the nucleic acid encoding a chondroitinase for secretion by the recombinant yeast strain. A person of ordinary skill in the art would have been motivated to make this modification because Khasa teaches that the anchoring signals are useful in various applications such as recombinant protein expression and secretion , and it therefore would be considered advantageous to incorporate an anchoring signal in addition to a secretion signal to promote secretion of the recombinantly expressed chondroitinase . As Kang teaches that enzymes with chondroitinase activity are used to digest chondroitin that has been produced by the recombinant cell, it would be of interest to ensure that the chondroitinase expressed by the recombinant cell is effectively secreted so that it can degrade the chondroitin. A skilled artisan would have had a reasonable expectation of success in making this modification because Khasa teaches that anchoring and secretion signals are both incorporated into fusion proteins to promote recombinant protein expression and secretion in yeast systems. Thus, a skilled artisan could reasonably expect success in incorporating an anchoring signal in addition to the secretion signal of the chondroitinase in the recombinant yeast cell of Kang and Amorim . Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Kang et al. as applied to claims 1, 5-6, 11, and 16-17 above, in view of Landstein et al., Virology ; 250(2):388-96. Kang teaches the recombinant yeast cell of claim 1 as set forth above. Kang does not teach that the nucleic acid encoding a polypeptide having a UDP-Glucose dehydrogenase activity is obtained or derived from Chlorella virus PBCV1 ( claim 8 ). Regarding claim 8, Landstein teaches the Chlorella virus PBCV-1 genome includes DNA encoding UDP-glucose dehydrogenase (UDP- GlcDH ) enzyme ( Landstein Abstract). Landstein teaches that the UDP- GlcDH converts UDP- Glc into UDP- GlcA and ORF A609L encodes a functional UDP- GlcDH enzyme ( Landstein pp. 388-389 para. 3; p. 390). It would have been obvious for a skilled artisan , before the effective filing date, to substitute the nucleic acid encoding the polypeptide having UDP-glucose dehydrogenase activity as taught by Kang with UDP- GlcDH from Chlorella virus PBCV-1 as taught by Landstein . This would be considered a simple substitution of one known element for another with an expectation of predictable results. Both the UDP- GlcDH taught by Kang ( tuaD ) and the UDP- GlcDH taught by Landstein have the same activity of converting UDP- Glc into UDP- GlcA . It would therefore have been obvious to substitute one of these enzymes for the other, as both have the same activity and have been successfully recombinantly expressed in a host organism, with a reasonable expectation of obtaining predictable results. Claim s 9 and 10 are rejected under 35 U.S.C. 103 as being unpatentable over Kang et al. as applied to claims 1, 5-6, 11, and 16-17 above, in view of Jing et al., Glycobiology ; 13(10):661-71. Kang teaches the recombinant yeast cell of claim 1 as set forth above. Kang does not teach that the nucleic acid encoding a polypeptide having a chondroitin synthase (HCOS) activity is a chimeric polypeptide ( claim 9 ), or that it is derived from Pasteurella multocida ( claim 10 ). Regarding claim 9, Jing teaches nucleic acid constructs encoding chimeric polypeptide s having chondroitin synthase (CS) activity and hyaluronan synthase (HAS) activity ( Jing Abstract; Table V; p. 670 “ Domain swapping constructs ”). Jing teaches that HASs polymerize the hyaluronan (HA) polysaccharide and CSs polymerize a polysaccharide composed of repeating β 4GlcUA- β 3GalNAc units (Jing p. 661 para. 1). Jing teaches that the chimeric enzymes comprising various combinations of HAS and CS residues have different combinations of CS, HAS, and GlcUA -transferase activities (Jing Table V, p. 666 “ Sugar transferase domain swapping between pmHAS and pmCS ”). Regarding claim 10, Jing teaches that the chimeric chondroitin synthase is from Pasteurella multocida (Jing Abstract). It would have been obvious for a skilled artisan , before the effective filing date, to modify the recombinant cell of Kang and utilize a chimeric polypeptide having chondroitinase activity, derived from Pasteurella multocida . Kang teaches a recombinant cell with a nucleic acid encoding a polypeptide with HCOS activity. It would have been obvious to a skilled artisan that the nucleic acid of Kang could be substituted for a nucleic acid encoding a chimeric polypeptide with HCOS activity as taught by Jing. While the nucleic acid of Kang is derived from E. coli, a skilled artisan would have been aware that a nucleic acid encoding a chimeric polypeptide from a different bacterium, P. multocida , could be incorporated in the recombinant yeast cell instead. A person of ordinary skill in the art would have been motivated to make this substitution because the chimeric polypeptide of Jing comprises both chondroitin synthase and hyaluronan synthase, and different residues in the chimeric proteins result in various combinations of CS, HAS, and GlcUA -transferase activities (Jing Table V). Thus, it would be considered advantageous to utilize a chimeric protein having chondroitin synthase activity as well as hyaluronan synthase or GlcUA -transferase activities, in order to polymerize different polysaccharide units and produce different polysaccharides (Jing “Introduction”). A skilled artisan would have had a reasonable expectation of success in making this substitution because the recombinant yeast cell of Kang comprises a nucleic acid encoding a bacterial chondroitin synthase, and thus could expect that a nucleic acid encoding a chimeric bacterial chondroitin synthase could similarly be incorporated in the yeast cell with predictable results. Claim 12 is rejected under 35 U.S.C. 103 as being unpatentable over Kang et al. as applied to claims 1, 5-6, 11, and 16-17 above, in view of Zhang et al., Metabolic Engineering ; 47:314-22. Kang teaches the recombinant yeast cell of claim 1 as set forth above. Kang does not teach that the cell further comprises at least one recombinant nucleic acid encoding a polypeptide having glutamine-fructose-6-phosphate amidotransferase (GFA1) a ctivity ( claim 12 ). Regarding claim 12, Zhang teaches E. coli cells for the m icrobial production of chondroitin (Zhang Abstract). Zhang teaches that fructose-6-phosphate i s the first common precursor in the synthesis of chondroitin and chondroitin-like polysaccharides (Zhang p. 316 Section 3.1; Fig. 1). Zhang teaches that Fru-6-P is converted to glucosamine-6-phosphate and by GlcN-6-P synthase ( GlmS ), which corresponds to EC: 2.6.1.16 (Zhang p. 316 Sections 2.9, 3.1). According to the instant specification, p. 71, p referred polypeptide s having glutamine-fructose-6-phosphate amidotransferase activity in the present invention are enzyme s having an EC number of EC 2.6.1.16 . Zhang teaches that overexpression of glmS enhanced the production of fructosylated chondroitin (Zhang p. 318 first partial para.). It would have been obvious for a skilled artisan , before the effective filing date, to modify the recombinant yeast cell of Kang with an additional nucleic acid encoding a protein having GFA1 activity. Kang teaches that the yeast cell comprises multiple nucleic acids encoding proteins that are critical for chondroitin production. Zhang teaches that GlmS , having glutamine-fructose-6-phosphate amidotransferase activity , results in enhanced production of chondroitin when recombinantly expressed in a host cell. Therefore, a skilled artisan would have found it obvious to additionally express this enzyme in the recombinant host cell of Zhang. A person of ordinary skill in the art would have been motivated to make this modification because the expression of the glmS gene in a recombinant host cell led to increased production of chondroitin as taught by Zhang. Therefore, it would be considered advantageous to incorporate this enzyme, which catalyzes a critical step in the process of chondroitin production, in a cell that produces chondroitin as taught by Kang. A skilled artisan would have had a reasonable expectation of success in making this modification because Kang teaches that numerous genes involved in the production of chondroitin are successfully expressed in a recombinant yeast cell, and Zhang teaches that a nucleic acid encoding a protein having glutamine-fructose-6-phosphate amidotransferase activity is successfully and beneficially expressed in a host cell for this same purpose. Therefore, an ordinary artisan could expect to successfully incorporate such a nucleic acid in the recombinant cell of Kang, to achieve predictable results. Claim 1 4 is rejected under 35 U.S.C. 103 as being unpatentable over Kang in view of Zhang as applied to claim 12 above, and further in view of Wang et al., Biotechnology letters ; 36(10):2023-8. Kang and Zhang teach the recombinant yeast cell of claim 1 2 as set forth above. Kang and Zhang do not teach that the nucleic acid encoding the polypeptide having glutamine-fructose-6-phosphate amidotransferase (GFA 1 ) activity is obtained or derived from Saccharomyces cerevisiae ( claim 1 4 ). Regarding claim 1 4 , Wang teaches that Glucosamine-6-phosphate (GlcN-6-P) synthase, also known as L-glutamine:D-fructose 6-phosphate amidotransferase (EC 2.6.1.16), is a key enzyme in the pathway of amino sugar biosynthesis (Wang p. 2023 para. 1). Wang teaches the characterization and expression of GlcN-6-P synthase from Saccharomyces cerevisiae in Pichia pastoris (Wang p. 2024 first full para.). It would have been obvious for a skilled artisan , before the effective filing date, to substitute the nucleic acid encoding the polypeptide having glutamine-fructose-6-phosphate amidotransferase activity as taught by Kang and Zhang with GFA1 from Saccharomyces cerevisiae as taught by Wang. This would be considered a simple substitution of one known element for another with an expectation of predictable results. Both the glmS enzyme taught by Zhang and the GFA1 taught by Wang have the activity of glutamine-fructose-6-phosphate amidotransferase . It would therefore have been obvious to substitute one of these enzymes for the other, as both have the same activity and have been successfully recombinantly expressed in a host organism, with a reasonable expectation of obtaining predictable results. Conclusion Claims 1-2, 4 -6, 8-12, 14, 16, and 17 are rejected. No claims are allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT EMILY F EIX whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)270-0808 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT M-F 8am-5pm ET . Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, FILLIN "SPE Name?" \* MERGEFORMAT Sharmila Landau can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT (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. /EMILY F EIX/ Examiner, Art Unit 1653 /SHARMILA G LANDAU/ Supervisory Patent Examiner, Art Unit 1653