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Purification and Characterization of Cell Wall Hydrolase from Alkalophilic Bacillus mutanolyticus YU5215

Authors
 OHK, SEUNG-HO  ;  SEUNG-WOO NAM  ;  JIN-MAN KIM  ;  YUN-JUNG YOO  ;  DONG-HOON BAI 
Citation
 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, Vol.14(6) : 1142-1149, 2004-12 
Journal Title
 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY 
ISSN
 1017-7825 
Issue Date
2004-12
Keywords
Cell wall hydrolase ; Streptococcus mutans ; Bacillus mutanolyticus YU5215 ; endopeptidase ; D-glutamic acid
Abstract
Streptococcus mutans has the capacity of inducing dental caries. Thus, to develop a novel way of preventing dental caries, a cell wall hydrolase-producing strain was isolated and its characteristics were investigated. Among 200 alkalophilic strains isolated from soil, 8 strains exhibited lytic activities against Streptococcus mutans. However, strain YU5215 with the highest cell wall hydrolase activity was selected for further study. Strain YU5215 was identified as a novel strain of Bacillus based on analyzing its 16S rDNA sequence and Bergey’s Manual of Systematic Bacteriology, and thus designated as Bacillus mutanolyticus YU5215. The optimal conditions for the production of the cell wall hydrolase from Bacillus mutanolyticus YU5215 consisted of glucose (0.8%), yeast extract (1.2%), polypeptone (0.5%), K2HPO4 (0.1%), MgSO4·7H2O (0.02%), and Na2CO3 (1.0%) at pH 10.0. Bacillus mutanolyticus YU5215 was cultured at 30oC for 72 h to produce the cell wall hydrolase, which was then purified by acetone precipitation and CM-agarose column chromatography. The molecular weight of the lytic enzyme was determined as 22,700 Da by SDS-PAGE. When the cell wall peptidoglycan of Streptococcus mutans was digested with the lytic enzyme, no increase in the reducing sugars was observed, while the free amino acids increased, indicating that the lytic enzyme had an endopeptidase-like property. The amino terminus of the cell wall peptidoglycan digested by the lytic enzyme was determined as a glutamic acid, while the lytic site of the lytic enzyme in the Streptococcus mutans peptidoglycan was identified as the peptide linkage of L-Ala and D-Glu.
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Appears in Collections:
2. College of Dentistry (치과대학) > Dept. of Oral Biology (구강생물학교실) > 1. Journal Papers
Yonsei Authors
Yoo, Yun Jung(유윤정) ORCID logo https://orcid.org/0000-0002-0045-9597
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/178817
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