Document Detail


Immobilization of recombinant thermostable beta-galactosidase from Bacillus stearothermophilus for lactose hydrolysis in milk.
MedLine Citation:
PMID:  19164659     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A recombinant thermostable beta-galactosidase from Bacillus stearothermophilus was immobilized onto chitosan using Tris(hydroxymethyl)phosphine (THP) and glutaraldehyde, and a packed bed reactor was utilized to hydrolyze lactose in milk. The thermostability and enzyme activity of THP-immobilized beta-galactosidase during storage was superior to that of free and glutaraldehyde-immobilized enzymes. The THP-immobilized beta-galactosidase showed greater relative activity in the presence of Ca(2+) than the free enzyme and was stable during the storage at 4 degrees C for 6 wk, whereas the free enzyme lost 31% of the initial activity under the same storage conditions. More than 80% of lactose hydrolysis in milk was achieved after 2 h of operation in the reactor. Therefore, THP-immobilized recombinant thermostable beta-galactosidase from Bacillus stearothermophilus has the potential for application in the production of lactose-hydrolyzed milk.
Authors:
W Chen; H Chen; Y Xia; J Yang; J Zhao; F Tian; H P Zhang; H Zhang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of dairy science     Volume:  92     ISSN:  1525-3198     ISO Abbreviation:  J. Dairy Sci.     Publication Date:  2009 Feb 
Date Detail:
Created Date:  2009-01-23     Completed Date:  2009-02-09     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985126R     Medline TA:  J Dairy Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  491-8     Citation Subset:  IM    
Affiliation:
State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, China. weichen@jiangnan.edu.cn
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MeSH Terms
Descriptor/Qualifier:
Animals
Food Handling
Geobacillus stearothermophilus / enzymology*
Hydrogen-Ion Concentration
Hydrolysis*
Ions / metabolism
Lactose / metabolism*
Metals / metabolism
Milk / chemistry*
Recombinant Proteins / metabolism*
Temperature
Time Factors
beta-Galactosidase / metabolism*
Chemical
Reg. No./Substance:
0/Ions; 0/Metals; 0/Recombinant Proteins; 63-42-3/Lactose; EC 3.2.1.23/beta-Galactosidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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