Abstract

The enzymatic hydrolysis of barley beta-glucan, konjac glucomannan and carboxymethyl cellulose by a beta-1,4-Dendoglucanase MeCel45A from blue mussel, Mytilus edulis, which belongs to subfamily B of glycoside hydrolase family 45 (GH45), was compared with GH45 members of subfamilies A (Humicola insolens HiCel45A), B (Trichoderma reesei TrCel45A) and C (Phanerochaete chrysosporium PcCel45A). Furthermore, the crystal structure of MeCel45A is reported. Initial rates and hydrolysis yields were determined by reducing sugar assays and product formation was characterized using NMR spectroscopy. The subfamily B and C enzymes exhibited mannanase activity, whereas the subfamily A member was uniquely able to produce monomeric glucose. All enzymes were confirmed to be inverting glycoside hydrolases. MeCel45A appears to be cold adapted by evolution, as it maintained 70% activity on cellohexaose at 4 degrees C relative to 30 degrees C, compared to 35% for TrCel45A. Both enzymes produced cellobiose and cellotetraose from cellohexaose, but TrCel45A additionally produced cellotriose.

Keywords

Endoglucanase; Blue mussel; Cel45A; GH45; Beta-glucan; Glucomannan

Published in

Carbohydrate Polymers
2022, Volume: 277, article number: 118771
Publisher: ELSEVIER SCI LTD

SLU Authors

• Okmane, Laura

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

• Nestor, Gustav

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

• Sandgren, Mats

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

• Ståhlberg, Jerry

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Biochemistry and Molecular Biology


Publication identifier

DOI: https://doi.org/10.1016/j.carbpol.2021.118771

Permanent link to this page (URI)

https://res.slu.se/id/publ/114514