Characterization of a novel thermostable GH16 β-1,3-1,4-glucanase from Streptomyces lividans with potential industrial applications

IF 3.9 3区生物学 Q2 BIOTECHNOLOGY & APPLIED MICROBIOLOGY

Enzyme and Microbial Technology Pub Date : 2027-01-01 Epub Date: 2026-10-13 DOI:10.1016/j.enzmictec.2026.110983

Jianwei Wang, Xin Wang, Wulong Jiang, Lin Xiang, Zhijian Deng, Rong Hu, Lianshun Wang, Yuting Cong, Li Wang, Yuan Wang, Jing Gu, Yanan Lu, Guojun Yang, Hua Wang

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引用次数: 0

Abstract

A novel GH16 β-1,3-1,4-glucanase, SlGH16, was identified from Streptomyces lividans and exhibits considerable thermostability and a broad pH tolerance, retaining appreciable activity under industrially relevant high-temperature and extreme pH conditions. SlGH16 preferentially hydrolyzes barley β-glucan to produce low-molecular-weight oligosaccharides (DP3–DP5), offering some potential for functional feed and oligosaccharide production. Integrative structural analyses, including AlphaFold3 modeling, molecular docking, and molecular dynamics simulations, revealed that two disulfide bonds (Cys161-Cys169, Cys181-Cys186) and the central aromatic residue Phe248 act as important stabilizing elements, preserving substrate-binding integrity and overall protein rigidity. Site-directed mutagenesis confirmed the important roles of these residues in catalytic efficiency and thermal resilience. The combination of moderate stability, precise substrate recognition, and efficient oligosaccharide generation positions SlGH16 as a promising candidate biocatalyst for high-temperature industrial applications. This study not only elucidates the structural determinants of GH16 enzyme thermostability but also provides a mechanistic reference for rational protein engineering aimed at enhancing enzyme performance under harsh processing conditions.

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一种具有工业应用潜力的新型lividans链霉菌GH16 β-1,3-1,4葡聚糖酶的表征

从lividans链霉菌中鉴定出一种新的GH16 β- 1,3,1,4 -葡聚糖酶SlGH16，该酶具有相当的热稳定性和广泛的pH耐受性，在工业相关的高温和极端pH条件下仍保持可观的活性。SlGH16优先水解大麦β-葡聚糖生成低分子量低聚糖（DP3-DP5），具有一定的功能性饲料和低聚糖生产潜力。综合结构分析，包括AlphaFold3建模，分子对接和分子动力学模拟，揭示了两个二硫键（Cys161-Cys169, Cys181-Cys186）和中心芳香残基Phe248是重要的稳定元素，保持了底物结合的完整性和整体蛋白质的刚性。定点诱变证实了这些残基在催化效率和热弹性方面的重要作用。SlGH16具有中等稳定性、精确的底物识别和高效的低聚糖生成，是一种有前途的高温工业应用候选生物催化剂。该研究不仅阐明了GH16酶热稳定性的结构决定因素，而且为在恶劣加工条件下提高酶性能的合理蛋白质工程提供了机制参考。

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来源期刊

Enzyme and Microbial Technology 生物-生物工程与应用微生物

CiteScore

7.60

自引率

5.90%

发文量

142

审稿时长

38 days

期刊介绍： Enzyme and Microbial Technology is an international, peer-reviewed journal publishing original research and reviews, of biotechnological significance and novelty, on basic and applied aspects of the science and technology of processes involving the use of enzymes, micro-organisms, animal cells and plant cells. We especially encourage submissions on: Biocatalysis and the use of Directed Evolution in Synthetic Biology and Biotechnology Biotechnological Production of New Bioactive Molecules, Biomaterials, Biopharmaceuticals, and Biofuels New Imaging Techniques and Biosensors, especially as applicable to Healthcare and Systems Biology New Biotechnological Approaches in Genomics, Proteomics and Metabolomics Metabolic Engineering, Biomolecular Engineering and Nanobiotechnology Manuscripts which report isolation, purification, immobilization or utilization of organisms or enzymes which are already well-described in the literature are not suitable for publication in EMT, unless their primary purpose is to report significant new findings or approaches which are of broad biotechnological importance. Similarly, manuscripts which report optimization studies on well-established processes are inappropriate. EMT does not accept papers dealing with mathematical modeling unless they report significant, new experimental data.