Characterization of a new acid stable exo-beta-1,3-glucanase of Rhizoctonia solani and its action on microbial polysaccharides.
A new acid stable exo-beta-1,3-glucanase of Rhizoctonia solani purified from a commercial source 'Kitarase-M', by a combination of ammonium sulfate precipitation, ion-exchange and gel filtration methods, had specific activity of 0.26 U/mg protein, Km and Vmax values of 0.78 mg/ml and 0.27 mM/min/mg protein, respectively. It had molecular weight of 62 kDa with optimum activity at 40 degrees C temperature and pH 5.0, with high stability at pH of 3-7. Unique amino acid sequence was found at N-terminal end. The substrate specificity studies confirmed that it is an exo-beta-1,3-glucanase. It could hydrolyze curdlan powder to release glucose.
Vijayendra
S V N
SV
Applied Microbiology Division, National Food Research Institute, Kan-nondai, 2-1-12, Tsukuba, Ibaraki 305-8642, Japan. svnvijayendra@yahoo.com
Kashiwagi
Yutaka
Y
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D043326:Glucan 1,3-beta-Glucosidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D011135:Polysaccharides, Bacterial / Q000378:metabolism; D012232:Rhizoctonia / Q000201:enzymology*; D020539:Sequence Analysis, Protein; D013379:Substrate Specificity
D011135:Polysaccharides, Bacterial; D043326:Glucan 1,3-beta-Glucosidase