Hydrolysis of oligosaccharides by a fungal α-galactosidase from fruiting bodies of a wild mushroom Leucopaxillus tricolor
In: Journal of Basic Microbiology, Jg. 58 (2018-09-05), S. 1043-1052
Online
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Zugriff:
A novel acidic α-galactosidase (EC 3.2.1.22) designated as Leucopaxillus tricolor α-galactosidase (LTG) has been purified to homogeneity from the fruiting bodies of L. tricolor to 855-fold with a specific activity of 956 U mg-1 by the application of chromatography and gel filtration. The molecular mass of LTG was estimated to be 60 kDa as determined by both SDS-PAGE and by gel filtration. The purified enzyme was identified by LC-MS/MS and four inner amino acid sequences were obtained. When 4-nitrophenyl α-D-glucopyranoside (pNPGal) was used as substrate, the optimal pH and optimal temperature of LTG were pH 5.0 and 50 °C, respectively. The enzyme activity was strongly inhibited by Hg2+ , Fe3 , Cu2+ , Cd2+ , and Mn2+ ions. The chemical modification agent N-bromosuccinimide (NBS) completely inhibited the enzyme activity of LTG, indicating the paramount importance of tryptophan residue(s) to its enzymatic activity. Besides, LTG displayed wide substrate diversity with activity toward a variety of substrates such as stachyose, raffinose, melibiose, locust bean gum, and guar gum. Given the good ability of degrading the non-digestible and flatulence-causing oligosaccharides, this fungus may become a useful source of α-galactosidase for multiple applications.
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Hydrolysis of oligosaccharides by a fungal α-galactosidase from fruiting bodies of a wild mushroom Leucopaxillus tricolor
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Autor/in / Beteiligte Person: | Xu, Lijing ; Geng, Xueran ; Fan, Jing ; Tzi Bun Ng ; Wang, Hexiang |
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Zeitschrift: | Journal of Basic Microbiology, Jg. 58 (2018-09-05), S. 1043-1052 |
Veröffentlichung: | Wiley, 2018 |
Medientyp: | unknown |
ISSN: | 0233-111X (print) |
DOI: | 10.1002/jobm.201800215 |
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