Purification and Characterization of X-Prolyl Dipeptidyl Aminopeptidase from Lactobacillus helveticus

doi:10.7506/spkx1002-6630-201317034

Abstract

Abstract:

X-prolyl dipeptidyl aminopeptidase (Pep X) from Lactobacillus helveticus was purified and characterized. The
Pep X was released from Lactobacillus helveticus cells by sonication. The cell-free extract was purified by ammonium
sulfate precipitation, chromatographed on Sephacryl S-300 HR and native-PAGE gel. The molecular mass of purified Pep X
was measured by SDS-PAGE. The specific activity of the enzyme was 62.24 U/mg. The purified Pep X had monomer
molecular mass of approximately 26 kD. Optimal activity was observed at pH 7.0 and 37 ℃. It was activated by Co2+
and inhibited by Zn2+, Ni2+, Mn2+ and Fe3+. It was a metallopeptidase and serine proteinase that was inhibited by EDTA
and PMSF.

Key words: X-prolyl dipeptidyl aminopeptidase (Pep X), purification, enzyme characterization

CLC Number:

TS201.3

GUO Yu-xing1，ZHU Qian1，ZHU Kun1，ZHOU Hui-min1，SUN Yang-ying1,2，ZENG Xiao-qun1,2，PAN Dao-dong1,2,*. Purification and Characterization of X-Prolyl Dipeptidyl Aminopeptidase from Lactobacillus helveticus[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201317034.

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Purification and Characterization of X-Prolyl Dipeptidyl Aminopeptidase from Lactobacillus helveticus

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