Novel immobilization of arginase I via cellulose-binding domain and its application in producing of L-Ornitine

作者：Li, M.^*; Yang, J.; Qu, H.; Zhang, Q.; Bai, F.; Bai, G.

来源：APPLIED BIOCHEMISTRY AND MICROBIOLOGY, 2014, 50(1): 43-48.

DOI：10.1134/S0003683813060112

• ENZYME
• ACID
• MICROSPHERES
• PROTEIN

The recombinant Escherichia coli strain pET35b-ARG, which overexpresses arginase I fused to a cellulose-binding domain (CBD), was developed. After preparing cellulose microspheres, arginase I was immobilized via the CBD of the fusion protein. Under optimal reaction conditions (40A degrees C, pH 9.5, 1 mM of Mn2+, 30 mu L/mL of immobilized enzyme, 30 g/L of L-Arg, and for 1 h), the conversion rate of L-Arg was 98.7%. After 7 reuses of 30 mu l of immobilized enzyme in 1 mL of catalytic solution, 153 mg of L-Orn with 97.3% purity was obtained. This indicated that the immobilization method was effective, feasible and could be used for the industrial production of L-Orn in the future.

• 出版日期2014-1
• 单位南开大学