Purification and Characterization of Trypsin from White Croaker (Argyrosomus argentatus)

doi:10.7506/spkx1002-6630-201613030

Abstract

Abstract:

An anionic trypsin (named as trypsin A) from the pyloric caeca of white croaker (Argyrosomus argentatus) was
purified by ammonium precipitation, DEAE-Sepharose Fast Flow anion exchange chromatography and Sephacryl S-200 gel
filtration chromatography. The characteristics of trypsin A were investigated. The results showed that trypsin A migrated as
a single protein band with a molecular weight of about 28 kD in SDS-PAGE. Trypsin A exhibited its optimal temperature at
50 ℃ and was stable below 65 ℃. Trypsin A revealed its optimal pH at 9.5 and was stable in the pH range from 9.5 to 11.0.
The purified trypsin A was analyzed by western blotting using anti-common carp trypsin antibody, and the result showed
that the active region of the trypsin was highly conservative. Serine proteinase inhibitors were effective against trypsin A.

Key words: white croaker, trypsin, separation and purification, enzymatic characteristics

CLC Number:

TS264.2

LI Huan, LI Ting, ZHAN Yunchao, DU Cuihong. Purification and Characterization of Trypsin from White Croaker (Argyrosomus argentatus)[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201613030.

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