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Transglycosylating and hydrolytic activities of the beta-mannosidase from Trichoderma reesei
KTH, Skolan för bioteknologi (BIO), Glykovetenskap.
Vise andre og tillknytning
2009 (engelsk)Inngår i: Biochimie, ISSN 0300-9084, E-ISSN 1638-6183, Vol. 91, nr 5, s. 632-638Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

A purified beta-mannosidase (EC 3.2.1.25) from the fungus Trichoderma reesei has been identified as a member of glycoside hydrolase family 2 through mass spectrometry analysis of tryptic peptides. In addition to hydrolysis, the enzyme catalyzes substrate transglycosylation with p-nitrophenyl beta-mannopyranoside. Structures of the major and minor products of this reaction were identified by NMR analysis as p-nitrophenyl mannobiosides and p-nitrophenyl mannotriosides containing beta-(1 -> 4) and beta-(1 -> 3) linkages. The rate of donor substrate hydrolysis increased in presence of acetonitrile and dimethylformamide, while transglycosylation was weakly suppressed by these organic solvents. Differential ultraviolet spectra of the protein indicate that a rearrangement of the hydrophobic environment of the active site following the addition of the organic solvents may be responsible for this hydrolytic activation.

sted, utgiver, år, opplag, sider
2009. Vol. 91, nr 5, s. 632-638
Emneord [en]
beta-Mannosidase, Transglycosylation, p-Nitrophenyl, beta-mannooligosaccharides, Organic solvents, rhodotorula-glutinis, enzymatic-synthesis, organic-solvents, identification, trisaccharide, purification, glucanase, alignment, complex, system
Identifikatorer
URN: urn:nbn:se:kth:diva-18437DOI: 10.1016/j.biochi.2009.03.009ISI: 000266193100008Scopus ID: 2-s2.0-64049097092OAI: oai:DiVA.org:kth-18437DiVA, id: diva2:336484
Merknad
QC 20100525Tilgjengelig fra: 2010-08-05 Laget: 2010-08-05 Sist oppdatert: 2017-12-12bibliografisk kontrollert

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