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While\n                      <jats:italic>Ideonella sakaiensis<\/jats:italic>\n                      PETase (IsPETase) and leaf-compost cutinase (LCC) efficiently depolymerize PET, many other PET-active hydrolases display stronger activity toward soluble PET intermediates such as bis- and mono(2-hydroxyethyl) terephthalate (BHET and MHET). Here, we describe a versatile carboxylesterase derived from\n                      <jats:italic>Bacillus halotolerans<\/jats:italic>\n                      (BhEstB). BhEstB is structurally related to BsEstB from\n                      <jats:italic>B. subtilis<\/jats:italic>\n                      but divergent from canonical PETases and most characterized MHETases, including IsMHETase, while clustering more closely with carboxylesterases such as TfCa. BhEstB displayed broad esterase activity toward\n                      <jats:italic>p<\/jats:italic>\n                      NP-esters, with maximum activity at pH 8 and 20\u201330\u00a0\u00b0C. Although it showed modest overall activity on the bulk polymer, BhEstB significantly outperformed the engineered variant LCC\n                      <jats:sup>ICCG<\/jats:sup>\n                      and the recently published archaeal feruloyl esterase PET46 in turning over BHET and MHET. BhEstB exhibits remarkably high activity toward BHET and MHET, achieving complete conversion of 50\u00a0mM BHET within 1\u00a0h at 30\u00a0\u00b0C (kcat\u2009=\u200915.57\u2009\u00b1\u20091.25\u00a0s\u207b\n                      <jats:sup>1<\/jats:sup>\n                      , Km\u2009=\u20096.54\u2009\u00b1\u20091.01\u00a0mM, corresponding to a catalytic efficiency of 2.38\u2009\u00d7\u200910\n                      <jats:sup>3<\/jats:sup>\n                      \u00a0M\u207b\n                      <jats:sup>1<\/jats:sup>\n                      \u00a0s\u207b\n                      <jats:sup>1<\/jats:sup>\n                      ) and subsequent efficient turnover of 39.8\u00a0mM MHET (77% (\u00b1\u20090.7%)) into terephthalic acid (TPA) within 24\u00a0h. These results identify BhEstB as one of the most efficient BHET-hydrolyzing enzymes characterized to date. Collectively, these findings establish BhEstB as a versatile BHET\/MHET active\n                      <jats:italic>Bacillus<\/jats:italic>\n                      carboxylesterase with modest activity toward commercial semi-crystalline PET powder, contributing to the expanding diversity of PET-intermediate-degrading enzymes.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Keypoints<\/jats:title>\n                    <jats:p>\n                      \u2022\n                      <jats:italic>BhEstB exhibits structural divergence from canonical PET esterases.<\/jats:italic>\n                    <\/jats:p>\n                    <jats:p>\n                      \u2022\n                      <jats:italic>BhEstB efficiently degrades significant amounts of BHET and MHET at 30\u00a0\u00b0C.<\/jats:italic>\n                    <\/jats:p>\n                    <jats:p>\n                      \u2022\n                      <jats:italic>BhEstB demonstrates moderate activity on PET powder at elevated temperatures.<\/jats:italic>\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1007\/s00253-026-14056-w","type":"journal-article","created":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T01:53:54Z","timestamp":1791510834000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["A versatile Bacillus esterase reveals a carboxylesterase blueprint for PET intermediate degradation"],"prefix":"10.1007","volume":"110","author":[{"given":"Hadjira","family":"Bounabi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bilal","family":"Yahiaoui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meriem","family":"Gasmi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meroua Safa","family":"Mechouche","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nico","family":"B\u00e4se","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marno","family":"Gurschke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rebecka","family":"Molitor","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pablo","family":"P\u00e9rez-Garc\u00eda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfgang R.","family":"Streit","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,10,9]]},"reference":[{"key":"14056_CR1","doi-asserted-by":"publisher","DOI":"10.1016\/j.chemosphere.2023.138394","volume":"326","author":"W Alloun","year":"2023","unstructured":"Alloun W, Berkani M, Benaissa A, Shavandi A, Gares M, Danesh C, Lakhdari D, Ghfar AA, Chaouche NK (2023) Waste valorization as low-cost media engineering for auxin production from the newly isolated Streptomyces rubrogriseus AW22: model development. 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