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

• Published in: Applied microbiology and biotechnology Vol. 108; no. 1; p. 216
• Main Authors: Xia, Yanwei, Wang, Wei, Wei, Yaning, Guo, Chuanxu, Song, Sisi, Cai, Siqi, Miao, Youzhi
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01.12.2024; Springer Nature B.V
• Subjects: Amino acids; Amino Acids - genetics; animal feeding; Biofuels; Biomedical and Life Sciences; Biotechnologically Relevant Enzymes and Proteins; Biotechnology; clarification (processing); Endo-1,4-beta Xylanases - metabolism; Enzyme Stability; Enzymes; Fruit juices; Fungi - metabolism; hydrogen; Hydrogen bonding; Hydrogen bonds; Life Sciences; Microbial Genetics and Genomics; Microbiology; Mutagenesis; Residues; Stability analysis; Statistical analysis; Temperature; Thermal stability; van der Waals forces; Xylanase; xylanases; GH10 xylanase; Thermostability; Acid stability; Filamentous fungi

Acidic xylanases are widely used in industries such as biofuels, animal feeding, and fruit juice clarification due to their tolerance to acidic environments. However, the factors controlling their acid stability, especially in GH10 xylanases, are only partially understood. In this study, we identifi...