Document Detail

Repeated-Batch Operation of Immobilized beta-Galactosidase Inclusion Bodies-Containing Escherichia coli Cell Reactor for Lactose Hydrolysis.
MedLine Citation:
PMID:  21952375     Owner:  NLM     Status:  Publisher    
In this study, we investigated the performance of an immobilized beta-galactosidase inclusion bodies-containing Escherichia coli cell reactor, where the cells were immobilized in alginate beads, which were then used in repeated-batch operations for the hydrolysis of o-nitrophenyl-beta-D-galactoside or lactose over the long-term. In particular, in the Tris buffer system, disintegration of the alginate beads was not observed during the operation, which was observed for the phosphate buffer system. The o-nitrophenyl-beta-Dgalactoside hydrolysis was operated successfully up to about 80 h, and the runs were successfully repeated at least eight times. In addition, hydrolysis of lactose was successfully carried out up to 240 h. Using Western blotting analyses, it was verified that the beta-galactosidase inclusion bodies were sustained in the alginate beads during the repeatedbatch operations. Consequently, we experimentally verified that beta-galactosidase inclusion bodies-containing Escherichia coli cells could be used in a repeated-batch reactor as a biocatalyst for the hydrolysis of o-nitrophenyl-beta-D-galactoside or lactose. It is probable that this approach can be applied to enzymatic synthesis reactions for other biotechnology applications, particularly reactions that require long-term and stable operation.
Ji-Hyeon Yeon; Kyung-Hwan Jung
Related Documents :
811665 - An endo-alpha1 leads to 6-d-mannanase from a soil bacterium. purification, properties, ...
21541045 - Design of new competitive dengue ns2b/ns3 protease inhibitors-a computational approach.
1653955 - The role of mannose in the receptor of the monocyte locomotion inhibitory factor produc...
8223705 - Glycosylation in golgi apparatus of early spermatids of rat. a high resolution lectin c...
22098575 - Conformational variability of organophosphorus hydrolase upon soman and paraoxon binding.
22966015 - Plasmin and chymotrypsin have distinct preferences for channel activating cleavage site...
Publication Detail:
Type:  -    
Journal Detail:
Title:  Journal of microbiology and biotechnology     Volume:  21     ISSN:  1738-8872     ISO Abbreviation:  -     Publication Date:  2011 Sep 
Date Detail:
Created Date:  2011-9-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9431852     Medline TA:  J Microbiol Biotechnol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  972-978     Citation Subset:  -    
Department of Biotechnology, Chungju National University, Jeungpyung, Chungbuk 368-701, Korea.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

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

Previous Document:  Mannitol Production by Leuconostoc citreum KACC 91348P Isolated from Kimchi.
Next Document:  Roles of Putative Sodium-Hydrogen Antiporter (SHA) Genes in S. coelicolor A3(2) Culture with pH Vari...