Unusual substrate specificity in GH family 12: structure–function analysis of glucanases Bgh12A and Xgh12B from Aspergillus cervinus, and Egh12 from Thielavia terrestris

In this study, we compared the properties and structures of three fungal GH12 enzymes: the strict endoglucanase Bgh12A and the xyloglucanase Xgh12B from Aspergillus cervinus, and the endoglucanase Egh12 from Thielavia terrestris combining activity on linear β-glucan and branched xyloglucan. Egh12 fr...

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Veröffentlicht in:	Applied microbiology and biotechnology 2022-02, Vol.106 (4), p.1493-1509
Hauptverfasser:	Rykov, Sergey V., Selimzyanova, Alina I., Nikolaeva, Alena Y., Lazarenko, Vladimir A., Tsurin, Nikita V., Akentyev, Philipp I., Zverlov, Vladimir V., Liebl, Wolfgang, Schwarz, Wolfgang H., Berezina, Oksana V.
Format:	Artikel
Sprache:	eng
Schlagworte:	Ascomycota Aspergillus Aspergillus cervinus Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology Cellulase - metabolism Comparative analysis Endoglucanase Enzymes Function analysis Fungi Glucan Homology Life Sciences Linkages Microbial enzymes Microbial Genetics and Genomics Microbiology Phylogeny Physiological aspects Pichia pastoris Residues Sordariales - metabolism Structural members Structure Structure-function relationships Substrate Specificity Substrates Substrates (Biochemistry) Thermal stability Thielavia terrestri Three dimensional models Xyloglucan Xyloglucanase β-Glucan
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