PMID: 9636315Jan 1, 1996Paper

Transplanting two unique beta-glucanase catalytic activities into one multienzyme, which forms glucose

Bio/technology
O OlsenD von Wettstein

Abstract

Endo cellulases of plant pathogenic erwinias degrade cellulose as well as the cellulosic domains of barley (1-3,1-4)-beta-glucan. Depolymerization of the latter substrate is mainly caused by (1-3,1-4)-beta-glucanases, which hydrolyze (1-4)-beta glycosidic linkages adjacent to (1-3)-beta linkages. To construct an enzyme for efficient degradation of barley (1-3,1-4)-beta-glucan, the sequence encoding the catalytic domain and interdomain linker of the cellulase from Erwinia carotovora subspecies atroseptica was fused to that for the heat stable Bacillus hybrid, H(A12-M) delta Y13 (1-3,1-4)-beta glucanase. The chimeric enzyme secreted from Escherichia coli cells did not remain covalently assembled as judged by SDS-PAGE. However, the glycosylated and intact enzyme (denoted CELGLU) is secreted from the yeast Pichia pastoris. CELGLU exhibits both cellulase and (1-3,1-4)-beta-glucanase catalytic activities, and was accordingly classified a true multienzyme. HPLC and NMR analyses revealed that among the products from CELGLU, di- and trimeric oligosaccharides were identical to those produced by the parental cellulase. Tetrameric oligosaccharides, derived from the (1-3,1-4)-beta-glucanase activity of CELGLU, were further degraded by the c...Continue Reading

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Citations

Dec 5, 2008·Journal of the American Chemical Society·Pamela Peralta-YahyaVirginia W Cornish
Jun 8, 2001·The Plant Journal : for Cell and Molecular Biology·M P CaspersV Cameron-Mills
Jan 13, 2000·European Journal of Biochemistry·B O PetersenK K Thomsen
Oct 28, 2006·Annual Review of Plant Biology·Diter von Wettstein
Dec 6, 2000·Proceedings of the National Academy of Sciences of the United States of America·D von WettsteinC G Kannangara
Jun 1, 1996·Critical Reviews in Biochemistry and Molecular Biology·P Béguin, M Lemaire
Nov 27, 2004·Journal of Molecular Recognition : JMR·Rachel Daly, Milton T W Hearn

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