{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T03:44:16Z","timestamp":1792122256028,"version":"4.4.0"},"reference-count":35,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T00:00:00Z","timestamp":1792022400000},"content-version":"vor","delay-in-days":14,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Macromolecular Bioscience"],"published-print":{"date-parts":[[2026,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>Recent advances in enzymatic polyester depolymerization have highlighted the potential of biocatalysis for sustainable plastic recycling. In contrast, efficient enzymatic strategies for polyamide (PA) degradation remain limited. Here, we investigate how complementary amidases influence product formation during the enzymatic treatment of bulk nylon\u20106 (PA6) and nylon\u20106,6 (PA66). Guided by previously established substrate preferences, enzyme combinations are designed to couple NylC\u2010mediated oligomer cleavage with downstream conversion by NylB or cyclic oligomer ring\u2010opening by NylA. Sequential enzyme treatments demonstrate efficient conversion of characteristic PA6\u2010 and PA66\u2010derived intermediates, while one\u2010pot systems enable coordinated downstream conversion at 34\u00b0C\u201340\u00b0C. For PA6, NylB efficiently converts the NylC\u2010generated 6\u2010aminohexanoic acid dimer to 6\u2010aminohexanoic acid, whereas for PA66, NylA selectively redirects accessible cyclic PA66\u2010derived species toward the corresponding linear repeat\u2010unit product. These changes in product distribution are not accompanied by a substantial increase in the overall amount of soluble polymer\u2010derived material. The detected soluble products represent less than 1% of the initial polymer mass under the investigated conditions, demonstrating that overall soluble product release remains limited. Together, these results show that complementary amidases can control downstream intermediate conversion and product selectivity during enzymatic nylon depolymerization.<\/jats:p>","DOI":"10.1002\/mabi.70274","type":"journal-article","created":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T02:56:33Z","timestamp":1792119393000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Cooperative Amidase Systems Control Product Selectivity During Enzymatic Nylon Depolymerization"],"prefix":"10.1002","volume":"26","author":[{"given":"Sukmanita","family":"Dewi","sequence":"first","affiliation":[{"name":"Institute of Macromolecular Chemistry Albert\u2010Ludwigs\u2010University of Freiburg  Freiburg 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