Purification and characterization of the extracellular aspartyl protease APSm1 from the phytopathogen fungus Stenocarpella maydis
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- 作者：Virginia Mandujano-Gonzá ; lez ; Alejandro Té ; llez-Jurado ; Miguel Angel Anducho-Reyes ; Ainhoa Arana-Cuenca ; Yuridia Mercado-Flores ; yuridiamercado@upp.edu.mx" class="auth_mail" title="E-mail the corresponding author ; yuridia_utsh@hotmail.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：Aspartyl protease ; Phytopathogenic fungus ; Stenocarpella maydis
- 刊名：Protein Expression and Purification
- 出版年：2016
- 出版时间：January 2016
- 年：2016
- 卷：117
- 期：Complete
- 页码：1-5
- 全文大小：513 K
文摘
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The extracellular protease APSm1 was purified to homogeneity from Stenocarpella maydis.
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The molecular weight of enzyme was estimated to be 56.8 kDa.
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Enzymatic activity toward hemoglobin was optimal at pH 2.0 and at 25 °C.
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Pepstatin A inhibited APSm1 activity, as the protein is in fact an aspartyl protease.
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The Km and Vmax values obtained were 0.514 mg/mL and 0.222 μmol/min, respectively, using hemoglobin as the substrate.