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In relation to this article, we declare that there is no conflict of interest.
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Received August 23, 2023
Accepted August 23, 2023
articles This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Expression and purification of beefy meaty peptide in Pichia pastoris

Key Laboratory of Food Nutrition and Safety, Tianjin University of Science & Technology, Ministry of Education, Tianjin 300457, China 1Beijing Kawin Bio-Tech Co., Ltd, Beijing, China 2Faculty of Sciences, Department of Home and Health Sciences, Allama Iqbal Open University, H-8, Islamabad Pakistan
Korean Journal of Chemical Engineering, March 2011, 28(3), 848-852(5), 10.1007/s11814-010-0439-5
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Abstract

We established a gene expression process to produce a flavor peptide in Pichia pastoris. The octapeptide Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala was isolated from beef digested by papain, known as “beefy meaty peptide” (BMP). It was considered a savory seasoning in previous literatures. To produce BMP by microorganisms, BMP expression structures encoding tandem repeats of the octapeptide were designed and cloned in E. coli DH5α, then integrated into_x000D_ the AOX1 gene of Pichia pastoris GS115. Clones containing different BMP-gene copies, with 4-copy, 8-copy, 12-copy and 16-copy, were obtained and expressed in Pichia pastoris GS115. For the ease of purification, 6×His tag was fused to the C-termini of the peptides. As a result, the fusion peptides were successfully purified by His-tag bind affinity resin. The BMP fusion peptides with expected sizes were secreted from the resulting strains of P. pastoris GS115.

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