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Functional Analysis of a Highly Active β-Glucanase from Bisporasp. MEY-1 Using Its C-terminally Truncated Mutant
- Source :
- Journal of Agricultural and Food Chemistry; August 2018, Vol. 66 Issue: 37 p9728-9737, 10p
- Publication Year :
- 2018
-
Abstract
- A β-1,3–1,4-glucanase-encoding gene, Bisglu16B, was identified in Bisporasp. MEY-1. The deduced BisGlu16B consists of an N-terminal signal peptide, a catalytic module of glycoside hydrolase family 16 (GH16), and a C-terminal serine/proline-rich module. After expression in Pichia pastorisGS115, the purified recombinant BisGlu16B showed maximal activity at pH 4.0 and 55 °C and had broad substrate specificity (β-1,3-/β-1,4-mixed, β-1,3-, β-1,4-, and β-1,6-linked glucan, and β-1,4-mannan). The enzyme possessed high specific activities toward barley β-glucan (34 700 U·mg–1), lichenan (23 900 U·mg–1), and laminarin (9 000 U·mg–1). After removing the C-terminal module, the truncated mutant, BisGlu16B-ΔC, retained similar enzymatic properties to the wild type but displayed significantly enhanced activities (up to 2.5-fold). Functional and structural analyses indicated that the C-terminal module plays a key role in the substrate binding of BisGlu16B. This study provided an excellent candidate glucanase for industrial purposes and revealed the functions of a C-terminal serine/proline-rich region.
Details
- Language :
- English
- ISSN :
- 00218561 and 15205118
- Volume :
- 66
- Issue :
- 37
- Database :
- Supplemental Index
- Journal :
- Journal of Agricultural and Food Chemistry
- Publication Type :
- Periodical
- Accession number :
- ejs46090633
- Full Text :
- https://doi.org/10.1021/acs.jafc.8b01928