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中国精品科技期刊2020
王周圆, 别小妹, 吕凤霞, 赵海珍, 陆兆新. 产黄青霉A4产胞外葡萄糖氧化酶发酵工艺优化[J]. 食品工业科技, 2015, (16): 217-221. DOI: 10.13386/j.issn1002-0306.2015.16.036
引用本文: 王周圆, 别小妹, 吕凤霞, 赵海珍, 陆兆新. 产黄青霉A4产胞外葡萄糖氧化酶发酵工艺优化[J]. 食品工业科技, 2015, (16): 217-221. DOI: 10.13386/j.issn1002-0306.2015.16.036
WANG Zhou-yuan, BIE Xiao-mei, LV Feng-xia, ZHAO Hai-zhen, LU Zhao-xin. Optimization of medium components and fermentation condition for extracellular glucose oxidase production by Penicillium chrysogenum A4[J]. Science and Technology of Food Industry, 2015, (16): 217-221. DOI: 10.13386/j.issn1002-0306.2015.16.036
Citation: WANG Zhou-yuan, BIE Xiao-mei, LV Feng-xia, ZHAO Hai-zhen, LU Zhao-xin. Optimization of medium components and fermentation condition for extracellular glucose oxidase production by Penicillium chrysogenum A4[J]. Science and Technology of Food Industry, 2015, (16): 217-221. DOI: 10.13386/j.issn1002-0306.2015.16.036

产黄青霉A4产胞外葡萄糖氧化酶发酵工艺优化

Optimization of medium components and fermentation condition for extracellular glucose oxidase production by Penicillium chrysogenum A4

  • 摘要: 以产黄青霉A4(Penicillium chrysogenum A4)作为葡萄糖氧化酶胞外酶生产菌株,通过单因素和正交设计实验,优化提高酶活的发酵培养基组分。结果表明:最佳发酵培养基成分组合为:碳源(葡萄糖)10%、有机氮源(麦芽浸粉)0.5%、无机氮源(Na NO3)1.7%。在最佳培养基上研究得到的发酵条件为:接种量1 m L、装液量50 m L、培养温度30℃、培养时间6 d。在此条件下,葡萄糖氧化酶活力提高到17.2 U/m L,为初始发酵酶活的17.2倍。 

     

    Abstract: Effects of different kinds of carbon source,organic nitrogen source and inorganic nitrogen source in medium on extracellular glucose oxidase(GOD) production by Penicillium chrysogenum A4 were studied by single-factor tests,respectively. The addition amount of glucose,malt extract and Na NO3 were optimized by orthogonal test. Results showed that the optimal addition amounts were as follow:glucose 10%,malt extract0.5%,Na NO31.7%. Based on the medium with the optimal components,the culture condition was also studied.Results showed that the optimal fermentation condition was as follow:1 m L spore suspension was incubated in50 m L of culture medium and 30 ℃ for 6 days. The glucose oxidase activity was 17.2 U/m L and 17.2 times that of initial enzyme activity.

     

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