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Role of Calcium Ion in the Thermostability of α-Amylase Produced from Bacillus Stearothermophilus

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Enzymes and Proteins from Thermophilic Microorganisms Structure and Function

Part of the book series: Experientia Supplementum ((EXS,volume 26))

Abstract

In 1961, Campbell and Manning provided one clue to elucidate the molecular basis for thermostability of the enzyme from thermophile(1–3). They reported that the α-amylase of B. stearothermophilus 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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Refference

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Author information

Authors and Affiliations

  1. Institute for Protein Research, Osaka University, Yamadakami, Suita, Osaka, Japan

    Katsuhide Yutani

Authors
  1. Katsuhide Yutani
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Editor information

Editors and Affiliations

  1. Eidgenössische Technische Hochschule, CH-8049, Zürich, Switzerland

    Herbert Zuber

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© 1976 Springer Basel AG

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Yutani, K. (1976). Role of Calcium Ion in the Thermostability of α-Amylase Produced from Bacillus Stearothermophilus . In: Zuber, H. (eds) Enzymes and Proteins from Thermophilic Microorganisms Structure and Function. Experientia Supplementum, vol 26. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-7675-9_8

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  • DOI: https://doi.org/10.1007/978-3-0348-7675-9_8

  • Publisher Name: Birkhäuser, Basel

  • Print ISBN: 978-3-0348-7677-3

  • Online ISBN: 978-3-0348-7675-9

  • eBook Packages: Springer Book Archive

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