Structural features of β-(1→4)-d-galactomannans of plant origin as a probe for β-(1→4)-mannanase polymeric substrate specificity

Abstract

Statistical modeling was applied for describing structural features of beta-(1 -> 4)-D-galactomannans. According to the model suggested theoretical ratios of limiting degrees of locust bean, tara gum and guar gum galactomannan conversions by two beta-(1 -> 4)-mannanases of different origin (Myceliophthora thermophila and Trichoderma reesei) were calculated. Then the enzymes were tested for enzymatic hydrolysis of three considered galactomannans. Experimentally observed results were compared with theoretically calculated ones. It was shown that T. reesei beta-mannanase attacks sequences of four and more unsubstituted mannopyranosyl residues in a row, while M. thermophila b-mannanase is a more specific enzyme and attacks sequences of five and more mannopyranosyl residues in a row. Considered statistical model and approach allows to characterize both galactomannan structures and enzyme requirements for regions of unsubstituted mannose residues for substrate hydrolysis. (C) 2012 Elsevier Ltd. All rights reserved.

Keywords

Galactomannan; beta-Mannanase; Enzymatic hydrolysis; Mannose; Galactose

Published in

Carbohydrate Research
2012, Volume: 352, pages: 65-69

UKÄ Subject classification

Biochemistry and Molecular Biology


Publication identifier

DOI: https://doi.org/10.1016/j.carres.2012.02.030

Permanent link to this page (URI)

https://res.slu.se/id/publ/84280