Heterologous expression, purification, and properties of a chymotrypsin inhibitor isolated from potatoes |
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| Authors: | I A Parfenov T A Revina N G Gerasimova G V Kladnitskaya T A Valueva |
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| Institution: | 1. Bakh Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia
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| Abstract: | The PKPIJ-B gene encoding a chymotrypsin inhibitor from a subfamily of potato Kunitz-type proteinase inhibitors (PKPI) in potatoes (Solanum tuberosum L. cv. Yubilei Zhukova) was cloned into a pET23a vector and then expressed in Escherichia coli. The recombinant PKPIJ-B protein obtained in the inclusion bodies was denatured, purified by high-performance liquid chromatography (HPLC) on Mono Q under denaturing conditions, and renaturated. The renaturated protein was additionally purified using HPLC on DEAE-ToyoPearl. The PKPIJ-B protein efficiently suppressed chymotrypsin activity, had a weaker effect on trypsin, and inhibited the growth and development of phytopathogenic microorganisms affecting potato plants. |
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