Purification and characterization of a novel heterodimer protease inhibitor from Streptomyces spp. VL J2 with potential biopesticidal activity against H. armigera
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- 作者：Kiran Marathe ; Sainath Kasar ; Ambalal Chaudhari ; Vijay Maheshwari ; vlmaheshwari@rediffmail.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：Protease inhibitor ; H. armigera ; Reverse zymography ; Streptomyces spp. ; Trypsin
- 刊名：Process Biochemistry
- 出版年：2016
- 出版时间：October 2016
- 年：2016
- 卷：51
- 期：10
- 页码：1650-1663
- 全文大小：3011 K
文摘
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A new heterodimeric proteinaceous protease inhibitor of approximately 38 kD was isolated from salt tolerant haloalkaliphilic Streptomyces spp.
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The purified protease inhibitor was found to be stable over a wide range of pH and temperature.
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The molecular weight, amino acids/groups required for activity and protease inhibition profile indicated it to be a serine protease inhibitor probably belonging to the serpin family.
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Kinetic data showed the nature of inhibition of trypsin by it to be non competitive type with a low inhibition constant.
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The isolated PI showed very good insecticidal activity against the polyphagous insect pest, Helicoverpa armigera affecting various stages of its life cycle and nutritional indices.