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• W2488374805 startingPage "2862" @default.
• W2488374805 abstract "Streptomyces thermolilacinus mannanase (StMan), which requires Ca 2+ for its enhanced thermal stability and hydrolysis activity, possesses two Ca 2+ ‐binding sites in loop6 and loop7. We evaluated the function of the Ca 2+ ‐binding site in loop7 and the hydrogen bond between residues Ser247 in loop6 and Asp279 in loop7. The Ca 2+ ‐binding in loop7 was involved only in thermal stability. Mutations of Ser247 or Asp279 retained the Ca 2+ ‐binding ability; however, mutants showed less thermal stability than StMan. Phylogenetic analysis indicated that most glycoside hydrolase family 5 subfamily 8 mannanases could be stabilized by Ca 2+ ; however, the mechanism of StMan thermal stability was found to be quite specific in some actinomycete mannanases." @default.
• W2488374805 created "2016-08-23" @default.
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• W2488374805 date "2016-08-23" @default.
• W2488374805 modified "2023-09-25" @default.
• W2488374805 title "Molecular insights into the mechanism of thermal stability of actinomycete mannanase" @default.
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• W2488374805 doi "https://doi.org/10.1002/1873-3468.12322" @default.
• W2488374805 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27447091" @default.
• W2488374805 hasPublicationYear "2016" @default.
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