Modulating the pH-activity profile of cellulase A from Cellulomonas fimi by replacement of surface residues
نویسندگان
چکیده
منابع مشابه
3-1,4-Glycanase from Cellulomonas fimi
The 0-1,4-glycanase Cex of the gram-positive bacterium Cellulomonas fimi is a glycoprotein comprising a C-terminal cellulose-binding domain connected to an N-terminal catalytic domain by a linker containing only prolyl and threonyl (PT) residues. Cex is also glycosylated by Streptomyces lividans. The glycosylation of Cex produced in both C. fimi and S. lividans protects the enzyme from proteoly...
متن کاملEnhancing the stability of xylanase from Cellulomonas fimi by cell-surface display on Escherichia coli.
AIMS The cell-surface display of Cex, which encodes xylanase and exoglucanase from Cellulomonas fimi, was constructed on Escherichia coli using PgsA as the anchor protein. Characterization of the cell-surface display of Cex was performed. METHODS AND RESULTS PgsA was fused to the N-terminus of Cex and six histidines were utilized as spacers between the targeting and anchor proteins. Successfu...
متن کاملMannan-degrading enzymes from Cellulomonas fimi.
The genes man26a and man2A from Cellulomonas fimi encode mannanase 26A (Man26A) and beta-mannosidase 2A (Man2A), respectively. Mature Man26A is a secreted, modular protein of 951 amino acids, comprising a catalytic module in family 26 of glycosyl hydrolases, an S-layer homology module, and two modules of unknown function. Exposure of Man26A produced by Escherichia coli to C. fimi protease gener...
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15 صفحه اولfrom linguistics to literature: a linguistic approach to the study of linguistic deviations in the turkish divan of shahriar
chapter i provides an overview of structural linguistics and touches upon the saussurean dichotomies with the final goal of exploring their relevance to the stylistic studies of literature. to provide evidence for the singificance of the study, chapter ii deals with the controversial issue of linguistics and literature, and presents opposing views which, at the same time, have been central to t...
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ژورنال
عنوان ژورنال: Protein Engineering Design and Selection
سال: 2011
ISSN: 1741-0126,1741-0134
DOI: 10.1093/protein/gzr004