Effect of the binding of bivalent ion to the calcium-binding site responsible for the thermal stability of actinomycete mannanase: Potential use in production of functional mannooligosaccharides
作者： Yuya Kumagai , Kayoko Kawakami , Misugi Uraji , Tadashi Hatanaka
DOI: 10.1016/J.MOLCATB.2013.05.001
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摘要: Abstract In a previous study, we determined that the calcium-binding site in catalytic domain of actinomycete mannanases is responsible for thermal stability [18] . To evaluate whether could bind to other bivalent ions, measured ability mannanase ions by using isothermal titration calorimetry (ITC) employing mutants StMandC (from Streptomyces thermolilacinus ) and TfMandC Thermobifida fusca deletion StDEDAAAdC TfDEDAAAdC. The bound with K 0.10 × 10 4 3.02 × 10 M −1 0.21 × 10 1.52 × 10 , respectively. Among tested was enhanced following order: magnesium, manganese, calcium. Magnesium barely mannanases. On hand, TfDEDAAAdC did not ions. From these results, showed involved binding association constant comprised negative enthalpy low entropy suitable ion
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