Biochemical characterization of alkaline peptidase CpyC from Aspergillus niger

  • CHENG Lei ,
  • WANG Zhengxiang
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  • 1(College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China)
    2(Key Lab of Industrial Microbiology of Tianjin Municipality, Tianjin 300457, China)

Received date: 2023-09-20

  Revised date: 2024-02-21

  Online published: 2024-12-27

Abstract

A proteolytic enzyme, CpyC, from Aspergillus niger was biochemically characterized.It contained a typical catalytic active site belonging to that of serine peptidase SB clan, with corresponding conserved amino acid residues Asp188, His226, and Ser381.Its conserved sequence or regions were similar to that of S08 class of the serine peptidase SB family, however, not completely identical to the existing family members' classification features.The purified recombinant CpyC showed its maximum activity at 50 ℃ and pH 8.0.The metal ion, Ca2+, showed the strongest activation effects on CpyC while Co2+ had the strongest inhibition effects.Its activity was strongly inhibited by phenylmethylsulfonyl fluoride, a specific serine protease inhibitor.The results suggested that protease CpyC from A.niger is an alkaline serine peptidase.CpyC could hydrolyze soybean protein isolate effectively and formed the main hydrolytes with polypeptide and oligopeptide, promoting its potential applications in protein bioprocessing.

Cite this article

CHENG Lei , WANG Zhengxiang . Biochemical characterization of alkaline peptidase CpyC from Aspergillus niger[J]. Food and Fermentation Industries, 2024 , 50(23) : 1 -6 . DOI: 10.13995/j.cnki.11-1802/ts.037431

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