Purification and characterization of chondroitinase ABC from Acinetobacter sp.C26
An extracellular chondroitinase ABC (ChSase ABC,EC.4.2.2.4) produced by cultivating Acinetobacter sp.C26,was purified to homogeneity from the supernatant by ammonium sulfate fractionation,Q-Sepharose Fast Flow and Sephadex G-100 chromatography.The 76kDa enzyme was purified 48.09-fold to hornogeneity with specific activity of 348.64U/mg,Using the chondroitin sulfate A (CS-A) as substrate,the maximal reaction rate (Vmax) and Michaelis-Menten constant (Km) of ChSase ABC were found to be 10.471 μmol/rnin/ml and 0.105 mg/ml,respectively.The enzyme showed t he highest activity at the optimal conditions of pH 6.0 and 42 ℃,respectively.This enzyme was stable at pH 5-10,5-9 and 5-7 at 4℃,37 ℃ and 42 ℃,respectively.Investigation about thermal stability of ChSase ABC displayed that it was stable at 37 ℃ ChSase ABC activity was increased in presence of Na+,K+,Mn2+,1,10-phenant hrolin and strongly inhibited by Cu2+,Hg2+,Al3+and SDS.These properties suggested that ChSase ABC from Acinetobacter sp.C26 bring promising prospects in medical and ind ustry applications.
Chondroitinase ABC Acinetobacter Purification Characterization
Changliang Zhu Jingliang Zhang Jing Zhang Yanhui Jiang Zhaopeng Shen Huashi Guan Xiaolu Jiang
School of Medicine and Pharmacy, Ocean University of China 5 Yushan Road, Qingdao 266003, PR China School of Medicine and Pharmacy, Ocean University of China 5 Yushan Road, Qingdao 266003, PR China;M College of Food Science and Engineering, Ocean University of China, 5 Yushan Road, Qingdao 266003, P
国内会议
青岛
英文
92-98
2017-09-20（万方平台首次上网日期，不代表论文的发表时间）