Purification and Characterization of α-1,4-Amylase in Body Wall of Sea Cucumber

doi:10.7506/spkx1002-6630-201505026

Abstract

Abstract:

α-1,4-Amylase was extracted and isolated from the body wall of sea cucumber by homogenization, salting out
with ammonium sulfate, dialysis, DEAE-52 anion exchange chromatography and Sephacryl S-300 gel chromatography
sequentially. The results showed that the purified enzyme had three subunit chains according to the SDS-PAGE, with
molecular weight of 420 kD; the optimum pH and temperature were 9.0 and 80 ℃; and the residual activity remained at least
38% after inactivation at 90 ℃ for 30 min. Therefore, this enzyme is a thermostable alkaline amylase. This amylase could be
strongly activated by K+, Fe3+ or Mn2+ and inhibited by Cu2+ or Ca2+.

Key words: sea cucumber, autolysis, amylase, isolation, purification, thermostability

CLC Number:

TS254.9

ZHANG Jie, ZHANG Yongqin*, LUO Caihua, LIU Zhengdong, CHENG Yuanfen, LU Feifei, ZHANG Tong. Purification and Characterization of α-1,4-Amylase in Body Wall of Sea Cucumber[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201505026.

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Purification and Characterization of α-1,4-Amylase in Body Wall of Sea Cucumber

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