Linked Life Data

21369984

Source:http://linkedlifedata.com/resource/pubmed/id/21369984

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pubmed-article:21369984pubmed:abstractTextBacillus 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).lld:pubmed
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pubmed-article:21369984pubmed:articleTitleCharacterization, gene cloning, and heterologous expression of ?-mannanase from a thermophilic Bacillus subtilis.lld:pubmed
pubmed-article:21369984pubmed:affiliationDepartment of Biotechnology, Mahidol University, Rama VI Rd., Bangkok, 10400, Thailand.lld:pubmed
pubmed-article:21369984pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:21369984pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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