Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2011-3-3
pubmed:databankReference
pubmed:abstractText
Bacillus subtilis BCC41051 producing a thermostable ?-mannanase was isolated from soybean meal-enriched soil and was unexpectedly found to be thermophilic in nature. The extracellular ?-mannanase (ManA) produced was hydrophilic, as it was not precipitated even with ammonium sulfate at 80% saturation. The estimated molecular weight of ManA was 38.0 kDa by SDS-PAGE with a pi value of 5.3. Optimal pH and temperature for mannan-hydrolyzing activity was 7.0 and 60°C, respectively. The enzyme was stable over a pH range of 5.0-11.5, and at temperatures of up to 60°C for 30 min, with more than 80% of its activity retained. ManA was strongly inhibited by Hg(2+) (1 mM), but was sensitive to other divalent ions to a lesser degree. The gene of ManA encoded a protein of 362 amino acid residues, with the first 26 residues identified as a signal peptide. High expression of recombinant ManA was achieved in both Escherichia coli BL21 (DE3) (415.18 U/ml) and B. megaterium UNcat (359 U/ml).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1976-3794
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
86-93
pubmed:meshHeading
pubmed-meshheading:21369984-Bacillus megaterium, pubmed-meshheading:21369984-Bacillus subtilis, pubmed-meshheading:21369984-Cations, Divalent, pubmed-meshheading:21369984-Chemical Fractionation, pubmed-meshheading:21369984-Cloning, Molecular, pubmed-meshheading:21369984-DNA, Bacterial, pubmed-meshheading:21369984-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:21369984-Enzyme Inhibitors, pubmed-meshheading:21369984-Enzyme Stability, pubmed-meshheading:21369984-Escherichia coli, pubmed-meshheading:21369984-Gene Expression, pubmed-meshheading:21369984-Hydrogen-Ion Concentration, pubmed-meshheading:21369984-Hydrophobic and Hydrophilic Interactions, pubmed-meshheading:21369984-Isoelectric Point, pubmed-meshheading:21369984-Mercury, pubmed-meshheading:21369984-Molecular Sequence Data, pubmed-meshheading:21369984-Molecular Weight, pubmed-meshheading:21369984-Protein Sorting Signals, pubmed-meshheading:21369984-Sequence Analysis, DNA, pubmed-meshheading:21369984-Soil Microbiology, pubmed-meshheading:21369984-Temperature, pubmed-meshheading:21369984-beta-Mannosidase
pubmed:year
2011
pubmed:articleTitle
Characterization, gene cloning, and heterologous expression of ?-mannanase from a thermophilic Bacillus subtilis.
pubmed:affiliation
Department of Biotechnology, Mahidol University, Rama VI Rd., Bangkok, 10400, Thailand.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't