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Enzymatic synthesis of beta-xylanase substrates: transglycosylation reactions of the beta-xylosidase from Aspergillus sp.

TitleEnzymatic synthesis of beta-xylanase substrates: transglycosylation reactions of the beta-xylosidase from Aspergillus sp.
Publication TypeJournal Article
Year of Publication2003
AuthorsEneyskaya, EV, Brumer, H, Backinowsky, LV, Ivanen, DR, Kulminskaya, AA, Shabalin, KA, Neustroev, KN
JournalCARBOHYDRATE RESEARCH
Volume338
Pagination313-325
Date PublishedFEB 7
Type of ArticleArticle
ISSN0008-6215
Abstract

A beta-D-xylosidase with molecular mass of 250 +/- 5 kDa consisting of two identical subunits was purified to homogeneity from a cultural filtrate of Aspergillus sp. The enzyme manifested high transglycosylation activity in transxylosylation with p-nitrophenyl P-D-xylopyranoside (PNP-X) as substrate, resulting in regio- and stereoselective synthesis of p-nitrophenyl (PNP) beta-(1 –> 4)-D-xylooligosaccharides with dp 2-7. All transfer products were isolated from the reaction mixtures by HPLC and their structures established by electrospray mass spectrometry and H-1 and C-13 NMR spectroscopy. The glycosides synthesised, beta-Xyl-1 –> (4-beta-Xyl-1 –>)(n)4-beta-Xyl-OC6H4NO2-p (n = 1 - 5), were tested as chromogenic substrates for family 10 beta-xylanase from Aspergillus orizae (XynA) and family 11 beta-xylanase I from Trichoderma reesei (XynT) by reversed-phase HPLC and UV-spectroscopy techniques. The action pattern of XynA against the foregoing PNP beta-(1 –> 4)-D-xylooligosaccharides differed from that of XynT in that the latter released PNP mainly from short PNP xylosides (dp 2 - 3) while the former liberated PNP from the entire set of substrates synthesised. (C) 2002 Elsevier Science Ltd. All rights reserved.

DOI10.1016/S0008-6215(02)00467-6