title: 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 β-(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 β-(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 β-mannanase attacks sequences of four and more unsubstituted mannopyranosyl residues in a row, while M. thermophila β-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.
authors.affiliation: Department of Chemistry, M.V. Lomonosov Moscow State University, Vorobievy Gory 1/11, Moscow 119899, Russia.
authors.forename: A A
authors.initials: AA
authors.lastname: Klyosov
authors.forename: G S
authors.initials: GS
authors.lastname: Dotsenko
authors.forename: S W A
authors.initials: SW
authors.lastname: Hinz
authors.forename: A P
authors.initials: AP
authors.lastname: Sinitsyn
mesh_terms: D005690:Galactose / Q000031:analogs & derivatives; D006868:Hydrolysis; D008351:Mannans / Q000737:chemistry*; D010944:Plants / Q000378:metabolism*; D020037:Sordariales / Q000201:enzymology; D013379:Substrate Specificity; D014242:Trichoderma / Q000201:enzymology; D044902:beta-Mannosidase / Q000378:metabolism*
chemical_list: D008351:Mannans; C012990:galactomannan; D044902:beta-Mannosidase; D005690:Galactose