Purification and characterization of a chitinase and a protease from Bacillus cereus TKU028 and their applications

• Main Authors: Tung-Yen Hsieh, 謝東諺
• Other Authors: 王三郎
• Format: Others
• Language: zh-TW
• Published: 2011
• Online Access: http://ndltd.ncl.edu.tw/handle/16027160193233580324

碩士 === 淡江大學 === 化學學系碩士班 === 99 === Bacillus cereus TKU028, a chitinase and protease-producing strain, was isolated from the soil in Taiwan, by using shrimp head powder (SHP) as the sole carbon/nitrogen source. A chitinase (CHT) and a protease (PRO) were purified by chitin affinity binding and casein affinity binding, respectively. The molecular masses of CHT and PRO determined by SDS- PAGE were approximately 40 kDa and 43 kDa, respectively. The optimum pH, optimum temperature, pH stability, and thermal stability of CHT and PRO were pH 5-6, 60 ℃, pH 5-8, and ≦60 ℃, and pH 9,50-60 ℃, pH 5-9, and ≦ 40℃, respectively. CHT was little inhibited by Mn2+ and EDTA, and PRO was inhibited by Cu2+ , EDTA, and 2 mM SDS. The chitinase-hydrolyzed products of subtract degradation were analyzed by HPLC at 1-48 h intervals. It was observed the major products are (GlcNAc)6. In addition, B. cereus TKU028 has unlimited potential to enhance the biodegradtion of shrimp shells in the seawater containing mangrove river sediment.