Document Detail


Bioproperties and purification of xylanase from Bacillus sp. YJ6.
MedLine Citation:
PMID:  19911836     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
To characterize the xylanase from Bacillus sp. YJ6, broth after 4 days incubation at 25 degrees C was collected and purified to electrophoretical homogeneity after Sephacryl S-100 HR chromatograph. About 3.5% recovery and 678.1 purification fold were achieved. The purified xylanase, with a Mw of 19 kDa, had an optimal pH and temperature at 5.0 and 50 degrees C, respectively, and was stable at pH 5.0-9.0 or <50 degrees C. It was inhibited by Cu2+, Fe3+, Hg2+, phenylmethyl sulfonyl fluoride (PMSF), N-tosyl-L-phenylalanine chloromethyl ketone (TPCK), N-ethylmaleimide (NEM), and leupeptin but activated by K+, Na+, Co2+, Mg2+, beta-mercaptoethanol (beta-ME), and glutathione (GSH). The purified xylanase had high specificity to beechwood, birchwood, and oat spelt xylans. The DNA fragment encoding this xylanase, corresponding to 213 amino acids, exhibited about 95% homology with seven strains of Bacillus in the NCBI database.
Authors:
Li-Jung Yin; Hsin-Hung Lin; Yen-I Chiang; Shann-Tzong Jiang
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of agricultural and food chemistry     Volume:  58     ISSN:  1520-5118     ISO Abbreviation:  J. Agric. Food Chem.     Publication Date:  2010 Jan 
Date Detail:
Created Date:  2010-01-06     Completed Date:  2010-03-22     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0374755     Medline TA:  J Agric Food Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  557-62     Citation Subset:  IM    
Affiliation:
Department of Sea Food Science, National Kaohsiung Marine University, No. 142 Hai-Chuan Rd. Nan-Tzu, Kaohsiung 81143, Taiwan. ljyin@mail.nkmu.edu.tw
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacillus / chemistry,  enzymology*,  genetics
Bacterial Proteins / chemistry*,  genetics,  isolation & purification*,  metabolism
Base Sequence
Endo-1,4-beta Xylanases / chemistry*,  genetics,  isolation & purification*,  metabolism
Enzyme Stability
Molecular Sequence Data
Molecular Weight
Substrate Specificity
Chemical
Reg. No./Substance:
0/Bacterial Proteins; EC 3.2.1.8/Endo-1,4-beta Xylanases

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


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