Purification and characterization of aminopeptidase from chicken intestine

被引：13

作者：

Jamadar, VK

Jamdar, SN

Dandekar, SP

Harikumar, P ^{[1
]}

机构：

[1] Bhabha Atom Res Ctr, Food Technol Div, Flesh Food Biochem Sect, Bombay 400085, Maharashtra, India

[2] KEM Hosp, Seth GS Med Coll, Dept Biochem, Bombay 400012, Maharashtra, India

来源：

JOURNAL OF FOOD SCIENCE | 2003年 / 68卷 / 02期

关键词：

aminopeptidase; purification; chicken intestine; manganese; puromycin;

D O I：

10.1111/j.1365-2621.2003.tb05691.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

An aminopeptidase was purified 839-fold with 15% recovery from chicken intestine by a procedure involving ion exchange, gel filtration,hydrophobic interaction and affinity chromatography. The enzyme is a heteridimer of subunits 94000 Da and,66000 Da. The substrate specificity of the enzyme was in the order ala > arg > leu-beta-naphthylamide. The enzyme was strongly inhibited by bestatin, puromycin, and 1, 10-phenanthroline. The aminopeptidase showed maximum activity at pH 6 and 40 to 50degreesC. The enzyme significantly differs from the hitherto known major classes of aminopeptidases from chicken tissues in terms of molecular weight and biochemical characteristics.

引用

页码：438 / 443

页数：6

共 32 条

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[2]

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[3] Debittering and hydrolysis of a tryptic hydrolysate of β-casein with purified general and proline specific aminopeptidases from Lactococcus lactis ssp cremoris AM2 [J].