کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
71145 48875 2007 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Characterization of the recombinant cellobiase from celG gene in the beta-glucoside utilization gene operon of Pectobacterium carotovorum subsp. carotovorum LY34
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی کاتالیزور
پیش نمایش صفحه اول مقاله
Characterization of the recombinant cellobiase from celG gene in the beta-glucoside utilization gene operon of Pectobacterium carotovorum subsp. carotovorum LY34
چکیده انگلیسی

A third cel operon containing celE, celF, and celG genes was isolated from Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34) genomic DNA using a cosmid library. The amino acid sequences of CelE and CelF shared high sequence identity with the cellobiose-specific PTS enzymes IIB and IIC, respectively. CelF contained the disaccharide binding region essential for acquiring cellobiose molecules. The amino acid sequence of CelG shared high sequence identity with various β-glucosidases (cellobiases) belonging to the glycosyl hydrolase family 1. Sequence and structural analysis also demonstrated that this cel operon differs from three operons previously reported from Pcc LY34, including bglTPB (accession number AY542524), ascGFB (accession number AY622309), and bglEFIA (accession number AY769096). In this study, the celF and celG genes were expressed in the presence of cellobiose. Purified CelG was estimated to be approximately 54 kDa by SDS-PAGE and was able to hydrolyze salicin, arbutin, pNPG, cellobiose, and MUG, and exhibited maximal activity at pH 5.0 to 40 °C. Two glutamic acid residues (Glu172 and Glu370) were shown to be essential for enzyme activity.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 47, Issues 1–2, 1 June 2007, Pages 91–98
نویسندگان
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