Keywords

Wheat Protein Disulfide Isomerase, Cloning, Expression, Enzymatic Properties

Abstract

Objective: To clone the wheat protein disulfide isomerase (wPDI) gene, realize its expression in E. coli and explore its enzymatic properties. Methods: Wpdi was obtained by reverse transcription and amplification using wheat seed total RNA as a template, and then prokaryotic expression was performed using pET-30b as the expression vector and Escherichia coli BL21 (DE3) as the host strain. The expression product was purified by metal chelation chromatography. Enzymatic properties studies were carried out. Results: The cloned gene has a full length of 1 548 bp and is 99% similar to the wpdi gene of the “Wyuna” variety wheat. The pET-30b-wpdi expression vector was constructed, and the optimal expression conditions for obtaining wPDI were: induction temperature 22¡ãC, induction time 6 h, and inducer concentration 0.5 mmol/L. The enzyme contains 4 thioredoxin domains, has a molecular mass of approximately 66.2 kD, and has disulfide bond reductase and isomerase activities as well as molecular chaperone activity. Conclusion: The study on the expression and enzymatic properties of recombinant wPDI provides a reference for the application of wPDI in pasta processing and other aspects.

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Original research done by Hou Yi, Liu Guang, Zhang Tingting, Li Lin, Wang Jingjing, Hu Songqing

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