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Purification and characterization of an acidic β-galactosidase from the hepatopancreas of the shrimpPenaeus japonicus (Crustacea: Decapoda)

✍ Scribed by Chuang, Nin-Nin ;Yang, Bei-Chia ;Yeh, Che-Chung

Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
630 KB
Volume
259
Category
Article
ISSN
0022-104X

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✦ Synopsis

Abstract

An acidic β‐galactosidase was purified approximately 2,500‐fold to homogeneity from the shrimp Penaeus japonicus. with a final specific activity of 4,000 units/mg of protein. SDS‐polyacrylamide gel electrophoresis revealed the monomers of the acidic β‐galactosidase to have a relative mass of 66,000. Since the active acidic β‐galactosidase was found to have a relative mass of 140,000 by Ferguson plot analysis, the purified enzyme was concluded to be dimeric. No protective polypeptide was identified in the final preparation of purified β‐galactosidase. The shrimp enzyme was found to be thermolabile. Upon heating at 56°C for 10 min, the enzyme lost 50% of its activity. The acidic β‐galactosidase had an isoelectric point (pI) of 4.6 ± 0.1 and the enzyme was sialyated. The shrimp enzyme had a pH optimum of 5.5 and its Km was 43 μM with 4‐methylumbelliferyl‐β‐D‐galactoside as substrate. The enzyme was inhibited by both Mn^++^ and Zn^++^ ions.

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