Partial purification and characterization of L-asparaginase from an endophytic Talaromyces pinophilus isolated from the rhizomes of Curcuma amada
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- 作者：Prajna Rao Krishnapuraa ; prajnaraok@gmail.com" class="auth_mail" title="E-mail the corresponding author ; Prasanna D. Belurb ; prsnbhat@gmail.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：Characterisation ; l-Asparaginase ; Purification ; Talaromyces pinophilus ; Thiol group
- 刊名：Journal of Molecular Catalysis B: Enzymatic
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：124
- 期：Complete
- 页码：83-91
- 全文大小：1359 K
文摘
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First report on characterization of l-asparaginase from an endophytic fungus.
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The enzyme is stable over a good range of pH and temperature.
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The enzyme is a heterodimer of 61.9 kDa and 39.1 kDa.
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The enzyme has a turnover number of 286.26 s−1.
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Cysteine residues play critical role in catalysis.