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Method for expressing human lysozyme-antibacterial peptide Parasin I fusion protein by virtue of pichia pastoris

A technology of human lysozyme and Pichia pastoris, applied in the field of biotechnology and genetic engineering, to achieve strong antibacterial activity and increase the effect of expression

Inactive Publication Date: 2015-05-20
SICHUAN AGRI UNIV
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Problems solved by technology

There is no report on the secretion and expression of lysozyme-antimicrobial peptide Parasin I fusion protein by Pichia pastoris

Method used

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  • Method for expressing human lysozyme-antibacterial peptide Parasin I fusion protein by virtue of pichia pastoris
  • Method for expressing human lysozyme-antibacterial peptide Parasin I fusion protein by virtue of pichia pastoris
  • Method for expressing human lysozyme-antibacterial peptide Parasin I fusion protein by virtue of pichia pastoris

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Experimental program
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Embodiment

[0036] The molecular biology experimental techniques used in the examples include PCR amplification, plasmid extraction, plasmid transformation, DNA fragment ligation, enzyme digestion, gel electrophoresis, etc., unless otherwise specified, generally operate in accordance with conventional methods. For details, please refer to "Molecular Cloning Experiment Guide (Third Edition) (Sambrook J, Russell DW, Janssen K, Argentine J. Huang Peitang et al. translation, 2002, Beijing: Science Press), or according to the conditions suggested by the manufacturer.

[0037] Pichia pastoris ( Pichia pastoris) X-33 was purchased from Invitrogen. The pPICZαA expression vector was purchased from Invitrogen. The pPICZαA expression vector (Invitrogen Company) was preserved in our laboratory.

[0038] 1. Obtaining the amino acid sequence of human lysozyme (SEQ ID NO:1):

[0039] The human lysozyme protein sequence (GenBank Accession No. AAC63078.1) was searched from the NCBI website.

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Abstract

The invention discloses a human lysozyme-antibacterial peptide Parasin I fusion protein and also provides a genetic engineering preparation method of the human lysozyme-antibacterial peptide Parasin I fusion protein. The invention further provides an antibacterial recombinant protein having high activity which is prepared by carrying out enzyme digestion on the fusion protein to achieve a stronger bacteriostatic effect on microorganisms, linking the human lysozyme-antibacterial peptide Parasin I gene to an efficient gene eukaryotic expression vector in a form of fusion protein and in the manner of gene recombination and further expressing the human lysozyme-antibacterial peptide Parasin I gene in saccharomycetes. The recombinant protein can be applied in an animal feed as an additive.

Description

technical field [0001] The invention relates to the fields of biotechnology and genetic engineering, in particular to a method for efficiently secreting and expressing recombinant human lysozyme-antimicrobial peptide Parasin I fusion protein using Pichia pastoris. Background technique [0002] Human lysozyme is a basic polypeptide composed of 130 amino acids with a molecular weight of 14700. It participates in the defense mechanism of the body, has the functions of anti-inflammation, anti-infection, anti-tumor and immune regulation, has high bacteriolytic activity and thermal stability, and is safer, non-irritating and side-effect-free than other lysozymes in clinical application. In addition, this enzyme is also widely used as a feed additive. [0003] Usually natural human lysozyme is extracted from human milk or placenta in a small amount, and the preparation materials are quite limited, which is far from meeting the needs of the market. In recent years, people have obt...

Claims

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Application Information

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IPC IPC(8): C12N15/81C12N15/62C12N15/56C12N15/12C12R1/84
Inventor 赵华汤加勇贾刚刘光芒陈小玲蔡景义
Owner SICHUAN AGRI UNIV
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