Journal of South China University of Technology(Natural Science Edition) ›› 2019, Vol. 47 ›› Issue (8): 57-63,70.doi: 10.12141/j.issn.1000-565X.180567

• Food Science & Technology • Previous Articles     Next Articles

Expression of Wheat Endoplasmic Reticulum Oxidoreductin 1 in Pichia pastoris

HU Songqing1 LI Wang1 CHEN Yu2 HOU Yi3   

  1. 1． School of Food Science and Engineering，South China University of Technology，Guangzhou 510640，Guangdong，China; 2． Guangdong Food Industry Institute，Guangzhou 510308，Guangdong，China; 3． School of Light Industry Science and Engineering，South China University of Technology，Guangzhou 510640，Guangdong，China
  • Received:2018-11-15 Revised:2018-12-28 Online:2019-08-25 Published:2019-08-01
  • Contact: 胡松青(1972-)，男，教授，博士生导师，主要从事食品蛋白质(酶)结构生物学、天然产物活性物质分离与功能研 E-mail:fesqhu@ scut.edu.cn
  • About author:胡松青(1972-)，男，教授，博士生导师，主要从事食品蛋白质(酶)结构生物学、天然产物活性物质分离与功能研
  • Supported by:
    Supported by the National Natural Science Foundation of China(31471691，31771906)

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Abstract: Wheat endoplasmic reticulum oxidoreductin 1 (wEro1) was expressed by Pichia pastoris recombinant to develop a healthy and natural novel biological flour improver． The wero1 gene was subcloned into the Pichia pastoris expression vector pPICZα A，and the secretory expression of wEro1 was realized in Pichia pastoris GS115． The yield of wEro1 reached (53. 24 ± 2. 11)U/mL after optimizing the induced expression conditions． The expressed products were purified by ammonium sulfate precipitation and anion exchange chromatography，and the enzymatic properties of wEro1 were investigated． The reasults show that wEro1 possesses thiol oxidizing activity catalyzing disulfide isomerase (PDI) with an optimum pH of 7. 5 and an optimum temperature of 30℃; the enzyme has good stability under low temperature and neutral pH conditions． Pichia pastoris recombinant wEro1 was added to flour to investigate its effect on flour processing quality． It was found that the ability of Pichia pastoris recombinant wEro1 to improve flour silty properties was stronger than that of E. coli recombinant wEro1．

Key words: wheat endoplasmic reticulum oxidoreductin 1, recombinant protein, sulfydryl oxidation, flour silty

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