Immobilization of recombinant thermostable β-galactosidase from Bacillus stearothermophilus for lactose hydrolysis in milk
Authors:
- W. ChenW. Chen
- H. ChenHCH. Chen
- Y. XiaYXY. Xia
- J. YangJYJ. Yang
- J. ZhaoJZJ. Zhao
- F. TianFTF. Tian
- H.P. ZhangHZH.P. Zhang
- 1 February 2009
- journal article
- research article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 92 (2) , 491-498
Abstract
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.Keywords
Funding Information
- National Natural Science Foundation of China (30670065)
- Project and Innovative Research Team in University (IRT0627)
- the National High Technology Research and Development Program of China (2007AA10Z316, 2007AA100604)
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