Purification and Function Analysis of beta-1,3-Glucanase from Paenibacillus sp.

• Main Authors: Jiun-Yu Chen, 陳俊宇
• Other Authors: Meng-Hsiao Meng
• Format: Others
• Language: zh-TW
• Published: 2001
• Online Access: http://ndltd.ncl.edu.tw/handle/75715880831773129395

碩士 === 國立中興大學 === 生物化學研究所 === 89 === Abstract A beta-1,3-glucanase was isolated from the culture supernatant of a Paenibacillus sp. grown on L broth medium containing 1 g pachyman (an insoluble b-1,3-glucan). The molecular mass of the enzyme was estimated to be 30-kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The 30-kDa emzyme was purified to homogeneity from the culture supernatant in this study. The property of this enzyme was examined. The enzyme belongs to a category of endo type 1,3-glucan glucanohydrolases. This enzyme was active at pH 5.0. The enzyme had activity on some insoluble beta-1,3-glucan such as curdlan, pachyman, Zymaose A, lichenan and no activity on others insoluble polysaccharide, but this enzyme bond to curdlan, cellulose and xylan. The optimum temperature of the reactions was 50℃when laminarin (a soluble beta-1,3-glucan) was used as the substrate at pH 5.0. The enzyme hydrolyzed lichenan (beta-1,3-1,4-glucan) more effectively than laminarin. A b-1,3-glucan, the substrate for the enzyme is a major component of the cell walls of pathogenic and potentially pathogenic fungi. The enzyme was lysed effecively fungal (Rhizoctonia solani AG-4) cell walls and resulted in the delay of fungi growth.