دورية أكاديمية
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A rumen-derived bifunctional glucanase/mannanase uncanonically releases oligosaccharides with a high degree of polymerization preferentially from branched substrates.

التفاصيل البيبلوغرافية
العنوان: A rumen-derived bifunctional glucanase/mannanase uncanonically releases oligosaccharides with a high degree of polymerization preferentially from branched substrates.
المؤلفون: Li N; Institute of Dairy Science, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China; Key Laboratory of Molecular Animal Nutrition, Ministry of Education, Zhejiang University, Hangzhou 310058, China., Han J; Institute of Dairy Science, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China; Key Laboratory of Molecular Animal Nutrition, Ministry of Education, Zhejiang University, Hangzhou 310058, China; College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, China., Zhou Y; College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, China., Zhang H; College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, China., Xu X; Institute of Dairy Science, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China; Key Laboratory of Molecular Animal Nutrition, Ministry of Education, Zhejiang University, Hangzhou 310058, China; College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, China., He B; State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China., Liu M; Key Laboratory of Specialty Agri-product Quality and Hazard Controlling Technology of Zhejiang Province, College of Life Sciences, China Jiliang University, Hangzhou 310018, China., Wang J; Institute of Dairy Science, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China; Key Laboratory of Molecular Animal Nutrition, Ministry of Education, Zhejiang University, Hangzhou 310058, China., Wang Q; Institute of Dairy Science, College of Animal Sciences, Zhejiang University, Hangzhou 310058, China; Key Laboratory of Molecular Animal Nutrition, Ministry of Education, Zhejiang University, Hangzhou 310058, China. Electronic address: Emirate14@zju.edu.cn.
المصدر: Carbohydrate polymers [Carbohydr Polym] 2024 Apr 15; Vol. 330, pp. 121828. Date of Electronic Publication: 2024 Jan 18.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Applied Science Publishers Country of Publication: England NLM ID: 8307156 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-1344 (Electronic) Linking ISSN: 01448617 NLM ISO Abbreviation: Carbohydr Polym Subsets: MEDLINE
أسماء مطبوعة: Publication: <1992-> : Barking : Elsevier Applied Science Publishers
Original Publication: London [Eng.] : Applied Science Publishers, c1981-
مواضيع طبية MeSH: Rumen*/metabolism , beta-Mannosidase*/metabolism, Animals ; Sheep ; Polymerization ; Oligosaccharides ; Polysaccharides ; Glycoside Hydrolases/metabolism ; Substrate Specificity ; Hydrolysis
مستخلص: Glycoside hydrolases (GHs) are known to depolymerize polysaccharides into oligo-/mono-saccharides, they are extensively used as additives for both animals feed and our food. Here we reported the characterization of IDSGH5-14(CD), a weakly-acidic mesophilic bifunctional mannanase/glucanase of GH5, originally isolated from sheep rumen microbes. Biochemical characterization studies revealed that IDSGH5-14(CD) exhibited preferential hydrolysis of mannan-like and glucan-like substrates. Interestingly, the enzyme exhibited significantly robust catalytic activity towards branched-substrates compared to linear polysaccharides (P < 0.05). Substrate hydrolysis pattern indicated that IDSGH5-14(CD) predominantly liberated oligosaccharides with a degree of polymerization (DP) of 3-7 as the end products, dramatically distinct from canonical endo-acting enzymes. Comparative modeling revealed that IDSGH5-14(CD) was mainly comprised of a (β/α) 8 -barrel-like structure with a spacious catalytic cleft on surface, facilitating the enzyme to target high-DP or branched oligosaccharides. Molecular dynamics (MD) simulations further suggested that the branched-ligand, 6 4 -α-D-galactosyl-mannohexose, was steadily accommodated within the catalytic pocket via a two-sided clamp formed by the aromatic residues. This study first reports a bifunctional GH5 enzyme that predominantly generates high-DP oligosaccharides, preferentially from branched-substrates. This provides novel insights into the catalytic mechanism and molecular underpinnings of polysaccharide depolymerization, with potential implications for feed additive development and high-DP oligosaccharides preparation.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
فهرسة مساهمة: Keywords: Bifunctionality; Glycoside hydrolase; High degree of polymerization; Rumen microbe
المشرفين على المادة: EC 3.2.1.25 (beta-Mannosidase)
0 (Oligosaccharides)
0 (Polysaccharides)
EC 3.2.1.- (Glycoside Hydrolases)
تواريخ الأحداث: Date Created: 20240217 Date Completed: 20240219 Latest Revision: 20240219
رمز التحديث: 20240219
DOI: 10.1016/j.carbpol.2024.121828
PMID: 38368107
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-1344
DOI:10.1016/j.carbpol.2024.121828