Clustered surface amino acid residues modulate the acid stability of GH10 xylanase in fungi

This study not only reported a series of valuable genes but also provided a range of modification targets for enhancing the acid stability of GH10 xylanases. KEY POINTS: • Five acid stable and thermostable GH10 xylanases were reported. • The key amino acid sites, mainly forming two enriched surface regions behind the enzyme active center, were identified responsible for acid stability of GH10 xylanases. • The finding revealed interactive amino acid sites, offering a pathway for synergistic enhancement of both acid stability and thermostability in GH10 xylanase modifications.PMID:38363378 | DOI:10.1007/s00253-024-13045-1

Source: Applied Microbiology and Biotechnology - February 16, 2024 Category: Microbiology Authors: Yanwei Xia Wei Wang Yaning Wei Chuanxu Guo Sisi Song Siqi Cai Youzhi Miao Source Type: research