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Titlebook: Enzymes and Proteins from Thermophilic Microorganisms Structure and Function; Proceedings of the I Herbert Zuber Conference proceedings 197

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Cheryl C. W. Ho,Ben Yuk Fai Fong,Ellen KuThermolysin is an extracellular proteolytic enzyme isolated from . (Endo, 1962). The enzyme is quite thermostable, retaining over half of its activity after being heated in an aqueous solution for an hour at 80°C, while at 65°C practically no inactivation occurs (Endo, 1962; Matsubara, 1967).
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The Structure and Stability of ThermolysinThermolysin is an extracellular proteolytic enzyme isolated from . (Endo, 1962). The enzyme is quite thermostable, retaining over half of its activity after being heated in an aqueous solution for an hour at 80°C, while at 65°C practically no inactivation occurs (Endo, 1962; Matsubara, 1967).
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Partial Characterization of a Thermophilic Actinomycete RenninThe thermophilic rennin isolated from a thermophilic actinomycete which was described previously by Laxer et al. (1972) and Pinsky et al. (1973) was further purified and characterized.
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Martin Klinthäll,Elisabeth Sundind that the α-amylase of . in the native state exists in a semi-random or random coiled and well hydrated molecule with slight extent of secondary structure formed by disulfide bonds (2). This less-ordered structure was postulated as the reason for thermostability of the enzyme.
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Modern Agencies — The Ideal Typeal strains of similar genera and species have been used for the purification of enzymes for comparison with those of mesophiles.. We have purified and investigated malate dehydrogenase (E.C.1.1.1.27). from . strain YT. (T.aq.MDH).
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