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内切葡聚糖酶基因工程菌pET-C36表达条件的研究 被引量:1

Research on Expression Conditions of Endoglucanase in the Recombinant E. coli Strain
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摘要 为了提高内切葡聚糖酶基因在大肠杆菌中的表达量,通过实验研究了重组菌Pet-C36的表达条件,结果表明重组菌的培养条件为:最适培养温度43℃,最适培养时间5 h,IPTG诱导终浓度0.1 mmol/L或乳糖诱导终浓度0.1%。基因工程菌在此条件下诱导培养后酶活力比未优化表达条件时提高了2倍,可达141.22 U/mL。 In order to improve the expression level of endoglucanase gene in E. coli, the expression conditions of the recombinant were studied in this experiment. The results showed that: the recombinant E. coli was incubated at 43 ℃ for 5 h, and when induced by 0.1 mmol/L IPTG or 0.1% lactose, its yield of endoglucanase can come to 141.22 U/mL which is about 2 times higher than that of the control.
出处 《四川农业大学学报》 CSCD 2007年第1期55-57,共3页 Journal of Sichuan Agricultural University
基金 四川省科技厅应用基础研究项目(05JY029-036-1)。
关键词 内切葡聚糖酶 重组菌株 表达条件 endoglucanase recombinant strain conditions of expression
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  • 1吴显荣,穆小民.纤维素酶分子生物学研究进展及趋向[J].生物工程进展,1994,14(4):25-27. 被引量:43
  • 2宋桂经,王冬,孙彩云,高培基.芽孢杆菌074碱性纤维素酶的研究——Ⅰ.菌种的分离、筛选及发酵条件[J].微生物学报,1995,35(1):38-44. 被引量:22
  • 3杜连起,李香艳.酶制剂在啤酒生产中的应用[J].酿酒科技,1996(3):48-49. 被引量:5
  • 4伊藤进 川合修次 等.-[J].日本农芸化学会志,1990,64(9):1445-1454.
  • 5中井良三 铃木哲.-[J].油化学,1988,37:1165-1168.
  • 6李育阳.基因表达技术[M].北京:科学出版社,2000..
  • 7奥斯伯F 布伦特R 金斯顿RE 等 颜子颖 王海林 编译.精编分子生物学实验指南[M].北京:科学出版社,1998.366-373.
  • 8Henrissat B, Driguez H, Viet C, et al.Synergism of cellulases from Trichoderma reesei in the degradation of cellulose [J]. Bio/Technology,1985,3:722~726.
  • 9Amann R I, Ludwig W,Schleifer K H.Phylogenetic identification and in situ detection of individual microbial cells without cultivation[J]. Microbiol Rev,1995,59:143~169.
  • 10Porteous L A,Armstrong J L. Recovery of bulk DNA from soil by a rapid, small-scale extraction method [J].Curr Microbiol,1991,22:345~348.

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  • 1李红梅,梅乐和,URLACHER VLADA,SCHMID ROLF D.催化吲哚生成靛蓝的细胞色素P450BM-3定向进化研究[J].生物化学与生物物理进展,2005,32(7):630-635. 被引量:14
  • 2韩学易,陈惠,吴琦,梁如玉,高凤菊,胥兵.产纤维素酶枯草芽孢杆菌C-36的产酶条件研究[J].四川农业大学学报,2006,24(2):178-181. 被引量:41
  • 3Fukuda T., Ishikawa T., Ogawa M., Shiraga S., Kato M.,Suye S., and Ueda M., 2006, Enhancement of cellulase activity by clones selected from the combinatorial library of the cellulose-binding domain by cell surface, Engineering, Biotechnology Progress, 22(4): 933-938.
  • 4Kiefer F., Arnold K., Kunzli M., Bordoli L., and Schwede T., 2009, The SWISS-MODEL repository and associated resources, Nucleic Acids Research, 37:387-392.
  • 5Kim Y.S., Jung H.C., and Pan J.G., 2000, Bacterial cell surface display of an enzyme library for selective screening of improved cellulase variants, Applied and Environmental Microbiology, 66:788-793.
  • 6Lin L., Meng X., Liu P.F., Hong Y.Z., Wu G.B., Huang X.L., Li C.C., Dong J.L., Xiao L., and Liu Z.D., 2009, Improved catalytic efficiency of endo-[3-1,4-glucanase from Bacillus subtilis BME-15 by directed evolution, Applied Microbiolgy Biotechnology, 82:671-679.
  • 7Liu W.J., Zhang X.Z., Zhang Z.M., and Zhang Y.H.P., 2010, Engineering of clostridium phytofermentans endoglucanase Cel5A for improved thermostability, Applied and Environmemtal Microbiology, 76(14): 4914-4917.
  • 8Nakazawa H., Okada K., Onodera T., Ogasawara W., Okada H., and Morikawa Y., 2009, Directed evolution of endoglucanase Ⅲ (Cel12A) fi:om Triehoderma reesei, AD10tied Microbiology and Bioteehnology ,83(4): 649-657.
  • 9Qin Y., Wei x., Song x., and Qu Y., 2008, Engineering endoglucanase Ⅱ from Triehoderma reesei to improve the catalytic efficiency at a higher pH optimum, Journal of Biotechnology, 135:190-195.
  • 10Wang T., Liu X.M., Yu Q., Zhang X., Qu Y.B., Gao P.J., and Wang T.H., 2005, Directed evolution for engineering pH profile of endoglucanase Ⅲ from Triehoderma reesei, Biomolecular Engineering, 22:89-94.

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