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PURIFICATION AND CHARACTERIZATION OF α-D-GALACTOSIDASE FROM TOMATO(PDF)

Chinese Journal of Applied & Environmental Biology[ISSN:1006-687X/CN:51-1482/Q]

Issue:
1996 04
Page:
369-375
Research Field:
Publishing date:

Info

Title:
PURIFICATION AND CHARACTERIZATION OF α-D-GALACTOSIDASE FROM TOMATO
Author(s):
Li Xingde Lu Yinghua
1. Chengdu Institute of Biology, Academia Sinica, Chengdu 610041;
2. Department of Biology, East China Normal University, Shanghai 200062
Keywords:
blood group conversiontomatoα-D-galactosidasepurilictionphysicochemical characters
CLC:
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PACS:
DOI:
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DocumentCode:

Abstract:
Tomato(Lycoporiscoum) was selected as raw material for purilyins α-D-galactosidase.Purified tomatoα-D-galactosidase was obtained by (NH4)2SO4 treatment,DEAE-Sephadex A-50 ion-exchange chromatography,Sephadex G-100 gel filtration and Melibiose-agnrose affinity chromatography.The results showed thata 5 290 fold purification of enzyme was obtained, its recovery rate was 45%,and the specific activity was52.9 U/mg.pro.The enzyme’s M, was 34 000 by SDS-G-PAGE.The tomato α-D-galactosidase was stableat pH 4.0-7.0 and tempetature 0-35℃.The enzyme hydrolysed substrate PNPG with the Km 0.11mmol/L,V,max = 67μmol·mg-1· min-1,optimum pH 5.1.The α-D-galactose is a competitive inhibitor ofthe enzyme.Metal ions CU2+.Zn2+.Mn2+.Fe3+.Ag+ and EDTA have no effects upon enzymology activity.

References

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Last Update: 1900-01-01