title: Optimization of culturing conditions of recombined Escherichia coli to produce umami octopeptide-containing protein.
abstract: Using synthesized peptides to verify the taste of natural peptides was probably the leading cause for tasting disputes regarding umami peptides. A novel method was developed to prepare the natural peptide which could be used to verify the taste of umami peptide. A controversial octopeptide was selected and gene engineering was used to structure its Escherichia coli. expressing vector. A response surface method was adopted to optimize the expression conditions of the recombinant protein. The results of SDS-PAGE for the recombinant protein indicated that the recombinant expression system was successfully structured. The fitting results of the response surface experiment showed that the OD600value was the key factor which influenced the expression of the recombinant protein. The optimal culturing process conditions predicted with the fitting model were an OD600value of 0.5, an IPTG concentration of 0.6mM, a culturing temperature of 28.75°C and a culturing time of 5h.
authors.affiliation: Key Laboratory of Meat Processing of Sichuan, Chengdu University, Chengdu 610106, China; The Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University, Chengdu 610106, China. Electronic address: yin.zhang@mail.scut.edu.cn.
authors.forename: Yin
authors.initials: Y
authors.lastname: Zhang
authors.affiliation: Key Laboratory of Meat Processing of Sichuan, Chengdu University, Chengdu 610106, China.
authors.forename: Xiong
authors.initials: X
authors.lastname: Wei
authors.affiliation: Key Laboratory of Meat Processing of Sichuan, Chengdu University, Chengdu 610106, China.
authors.forename: Zhou
authors.initials: Z
authors.lastname: Lu
authors.affiliation: Department of Biological and Agricultural Engineering, University of California, Davis, One Shields Avenue, Davis, CA 95616, USA; Healthy Processed Foods Research Unit, USDA-ARS-WRRC, 800 Buchanan St., Albany, CA 94710, USA.
authors.forename: Zhongli
authors.initials: Z
authors.lastname: Pan
authors.affiliation: Key Laboratory of Meat Processing of Sichuan, Chengdu University, Chengdu 610106, China.
authors.forename: Xinhua
authors.initials: X
authors.lastname: Gou
authors.affiliation: Department of Biological and Agricultural Engineering, University of California, Davis, One Shields Avenue, Davis, CA 95616, USA.
authors.forename: Chandrasekar
authors.initials: C
authors.lastname: Venkitasamy
authors.affiliation: Key Laboratory of Meat Processing of Sichuan, Chengdu University, Chengdu 610106, China.
authors.forename: Siya
authors.initials: S
authors.lastname: Guo
authors.affiliation: Key Laboratory of Meat Processing of Sichuan, Chengdu University, Chengdu 610106, China.
authors.forename: Liming
authors.initials: L
authors.lastname: Zhao
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005421:Flavoring Agents / Q000378:metabolism*; D015870:Gene Expression; D005818:Genetic Engineering; D010455:Peptides / Q000032:analysis / Q000235:genetics* / Q000378:metabolism; D011994:Recombinant Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D013696:Temperature
chemical_list: D005421:Flavoring Agents; D010455:Peptides; D011994:Recombinant Proteins
keywords: Engineering bacteria; Escherichia coli; Octopeptide; Umami peptides