Recombinant Expression of Bioactive Peptides: A Review

Abstract:

There is a wide source of bioactive peptides and the preparation methods of it are various. It is a novel process that preparing bioactive peptides by genetic engineering. In this paper, the expression system of bioactive peptides is discussed and its research progress is introduced.

• Periodical: Advanced Materials Research (Volumes 881-883)
• Pages: 331-334
• DOI: https://doi.org/10.4028/www.scientific.net/AMR.881-883.331
• Online since: January 2014
• Authors: Rong Liang, Mei Shuo Zhang, Song Yi Lin*
• Keywords: Expression System, Fusion Expression, Genetic Engineering, Peptide, Tandem Expression

References

[1] D. Agyei, M. K. Danquah, Rethinking food-derived bioactive peptides for antimicrobial and immunomodulatory activities, Trends Food Sci. Tech. 23 (2012) 62-69.

DOI: 10.1016/j.tifs.2011.08.010

[2] A. B. Ingham, R. J. Moore, Recombinant production of antimicrobial peptides in heterologous microbial systems, Biotechnol. Appl. Biochem. 47 (2007) 1–9.

DOI: 10.1042/ba20060207

[3] Y. W. Li, B. Li, J. G. He, et al., Quantitative structure–activity relationship study of antioxidative peptide by using different sets of amino acids descriptors, J. Mol Struct. 998 (2011) 53–61.

DOI: 10.1016/j.molstruc.2011.05.011

[4] A. Durak, B. Baraniak, A. Jakubczyk, et al., Biologically active peptides obtained by enzymatic hydrolysis of Adzuki bean seeds, Food Chem. 141 (2013) 2177–2183.

DOI: 10.1016/j.foodchem.2013.05.012

[5] E. K. Kim, S. J. Lee, B. T. Jeon, et al., Purification and characterisation of antioxidative peptides from enzymatic hydrolysates of venison proteinFood Chem. 114 (2009) 1365–1370.

DOI: 10.1016/j.foodchem.2008.11.035

[6] X. X. Xu, F. L. Jin, X. Q. Yu, et al., Expression and purification of a recombinant antibacterial peptide, cecropin, from Escherichia coli, Protein Expres. Purif. 53 (2007) 293–301.

DOI: 10.1016/j.pep.2006.12.020

[7] D. M. Floss, K. Schallau, R. J. Stefan, et al., Elastin-like polypeptides revolutionize recombinant protein expression and their biomedical application, Trends Biotechnol. 28(2009) 37–45.

DOI: 10.1016/j.tibtech.2009.10.004

[8] K. Yang, Y. J. Su, J. H. Li, et al., Expression and purification of the antimicrobial peptide cecropin AD by fusion with cationic elastin-like polypeptides, Protein Expres. Purif. 85 (2012) 200–203.

DOI: 10.1016/j.pep.2012.04.007

[9] Z. O. Shenkarev, Pavel V. Panteleev, Sergey V. Balandin, et al., Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfishAurelia aurita, Biochem. Bioph. Res. Co. 429 (2012) 63–69.

DOI: 10.1016/j.bbrc.2012.10.092

[10] H. Peng, M. Yang, W. S. Huang, et al., Soluble expression and purification of a crab antimicrobial peptide scygonadin in different expression plasmids and analysis of its antimicrobial activity, Protein Expres. Purif. 70 (2010) 109–115.

DOI: 10.1016/j.pep.2009.09.008

[11] W. Cao, Y. X. Zhou, Y. S. Ma, et al., Expression and puriWcation of antimicrobial peptide adenoregulin with C-amidated terminus in Escherichia coli, Protein Expres. Purif. 40 (2005) 404–410.

DOI: 10.1016/j.pep.2004.12.007

[12] B. Srinivasulu, R. Syvitski, J. K. Seo, et al., Expression, purification and structural characterization of recombinant hepcidin, an antimicrobial peptide identified in Japanese flounder, Paralichthys olivaceus, Protein Expres. Purif. 61 (2008).

DOI: 10.1016/j.pep.2008.05.012

[13] H. H. Hou, W. L. Yan, K. X. Du, et al., Construction and expression of an antimicrobial peptide scolopin 1 from the centipede venoms ofScolopendra subspinipes mutilansin Escherichia coli using SUMO fusion partner, Protein Expres. Purif. 92 (2013).

DOI: 10.1016/j.pep.2013.10.004

[14] X. X. Xu, F. L. Jin, X. Q. Yu, et al., Expression and purification of a recombinant antibacterial peptide, cecropin, from Escherichia coli, Protein Expres. Purif. 53 (2007) 293–301.

DOI: 10.1016/j.pep.2006.12.020

[15] R. A. Aleinein, R. Hamoud, H. Schäfer, et al., Molecular cloning and expression of ranalexin, a bioactive antimicrobial peptide from Rana catesbeiana in Escherichia coli and assessments of its biological activities, Appl Microbiol Biotechnol. 97 (2013).

DOI: 10.1007/s00253-012-4441-1

[16] L. Huang, H. L. Ma, Y. L. Li, et al., Antihypertensive activity of recombinant peptide IYPR expressed in Escherichia coli as inclusion bodies, Protein Expres. Purif. 83 (2012) 15–20.

DOI: 10.1016/j.pep.2012.02.004

[17] D. Liu, H. Y. Sun, L. J. Zhang, etal, High-Level Expression of Milk-Derived Antihypertensive Peptide in Escherichia coli and Its Bioactivity, J. Agric. Food Chem. 55 (2007) 5109−5112.

DOI: 10.1021/jf0703248

[18] F. Fan, Y. M. Wu, J. X. Liu, Expression and purification of two different antimicrobial peptides, PR-39 and Protegrin-1 in Escherichia coli, Protein Expres. Purif. 73 (2010) 147–151.

DOI: 10.1016/j.pep.2010.05.012

[19] T. J. Park, J. S. Kim, S. S. Choi, et al., Cloning, expression, isotope labeling, purification, and characterization of bovine antimicrobial peptide, lactophoricin in Escherichia coli, Protein Expres. Purif. 65 (2009) 23–29.

DOI: 10.1016/j.pep.2008.12.009

[20] J. Zhang, Y.L. Yang, D. Teng, et al., Expression of plectasin in Pichia pastoris and its characterization as a new antimicrobial peptide against Staphyloccocus and Streptococcus, Protein Expres. Purif. 78 (2011) 189–196.

DOI: 10.1016/j.pep.2011.04.014

[21] A. K. P. Vadhana, P. Samuel, R.M. Berin, et al., Improved secretion of Candida antarctica lipase B with its native signal peptide in Pichia pastoris, Enzyme Microb. Tech. 52 (2013) 177–183.

DOI: 10.1016/j.enzmictec.2013.01.001

[22] L. Wang, C. E. Lai, Q. F. Wu, et al., Production and characterization of a novel antimicrobial peptide HKABF by Pichia pastoris, Process Biochem. 43 (2008) 1124–1131.

DOI: 10.1016/j.procbio.2008.06.009