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A β-galactosidase from chick pea (Cicer arietinum) seeds: Its purification, biochemical properties and industrial applications.
MedLine Citation:
PMID:  23107735     Owner:  NLM     Status:  In-Data-Review    
A β-galactosidase from Cicer arietinum seeds has been purified to apparent electrophoretic homogeneity using a combination of various fractionation and chromatographic techniques, giving a final specific activity of 220unitsmg(-1), with approximately 1840 fold purification. Analysis of the protein by SDS-PAGE revealed two subunits with molecular masses of 48 and 38kDa, respectively. These bands were further confirmed with LC-MS/MS, indicating that Chick pea β-galactosidase (CpGAL) is a heterodimer. Molecular mass was determined to be 85kDa by Superose-12 FPLC column, which is in agreement with the molecular mass suggested by mass spectroscopy to be 83kDa. The optimum pH of the enzyme was 2.8 and it hydrolysed o-nitrophenyl β-d galactopyranoside (ONPG) with a K(m) value of 1.73mM at 37°C. The energy of activation (E(a)) calculated in the range of 35 to 60°C, using Arrhenius equation, was determined to be 11.32kcalmol(-1). The enzyme could also hydrolyse lactose, with an optimum pH of 4.0 at 40°C. K(m) and E(a) for lactose hydrolysis was found to be 10mM and 10.57kcalmol(-1), respectively. The enzyme was found to be comparatively thermostable showing maximum activity at 60°C for both ONPG and lactose. Galactose was found to be the competitive inhibitor. β-Galactosidase also exhibited glycoproteineous properties when applied on Con-A Sepharose column. The enzyme was localised in germinated seeds with X-gal activity staining and shown to be expressed prominently at grown radical tip and seed coat. Sequence alignment of CpGAL with other known plant β-galactosidase showed high amino acid sequence homology.
Devesh Kishore; Arvind M Kayastha
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Publication Detail:
Type:  Journal Article     Date:  2012-03-15
Journal Detail:
Title:  Food chemistry     Volume:  134     ISSN:  0308-8146     ISO Abbreviation:  Food Chem     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-10-30     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7702639     Medline TA:  Food Chem     Country:  England    
Other Details:
Languages:  eng     Pagination:  1113-22     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Ltd. All rights reserved.
School of Biotechnology, Faculty of Science, Banaras Hindu University, Varanasi 221005, India.
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