Biotechnology Bulletin ›› 2015, Vol. 31 ›› Issue (8): 193-199.doi: 10.13560/j.cnki.biotech.bull.1985.2015.08.028

• Research report • Previous Articles     Next Articles

A Study on Transesterification and Acid-resistant Antiprotease of Carboxypeptidase in Porcine Pancreas

Feng Shiyuan, Sun Tongwei, Mou Huiyan, Zhang Huitu, Lu Fuping   

  1. Tianjinn Key Laboratory of Industrial Microbiology,Key Laboratory of Industrial Fermentation Microbiology Ministry of Education,College of Biotechnology,Tianjin University of Science&Technology,Tianjin 300457
  • Received:2015-03-20 Online:2015-08-21 Published:2015-08-22

Abstract: Carboxypeptidase is a kind of protease that cleaves the peptide bond of an amino acid residue at the C-terminal end. It can be used in feed additives, and promotes the growth of livestock and poultry. A carboxypeptidase A1(CPA1)was obtained from porcine pancreas, and it can hydrolyze proteins and decompose oils. It showed the specific activity as 53.14 U/mg and 22.4 U/mg when casein and olive oil used as substrate, respectively. The CPA1’s relative activity reached 95.65% and 78.14% respectively after the treatment of pH2.0 acidic and trypsin. The results indicate that the CPA1 has the function of transesterification and the feature of distinct acid-resistant antiprotease.

Key words: carboxypeptidase A1, function of transesterification, acid-resistant antiprotease