藉基因工程產製天然抗菌物質乳鐵蛋白素(1/2)
Date Issued
2003
Date
2003
Author(s)
林慶文
DOI
912313B002378
Abstract
Bovine lactoferrin is a transferrin protein found
in milk, which has many biological functions.
Lactoferricin is a short fragment from the
N-terminus of lactoferrin. This peptide is about
25 amino acids. Lactoferricin is generated upon
gastric pepsin cleavage of lactoferrin in
mammalian animals. This peptide is much
more effective in antibacterial properties than
lactoferrin. And we could use the peptide to
develop new style probiotic products. Our
study is focus on the generation of the
recombinant yeast, Pichia pastoris, containing
the bovine lactoferricin gene fragment and the
feasibility of large-scale production. First, we
got synthetic lactoferricin and it’s antibacterial
core peptide of different species by peptide
synthesis, and then tested the antimicrobial
activities against Escherichia coli,
Staphylococcus aureus and Candida albicans.
Results revealed that the bovine lactoferricin
and its antibacterial core peptide show the
better ability of antimicrobial than the others.
We selected 11-amino acids antibacterial core
peptide of bovine lactoferricin, which has the
same antibacterial activity as the native
lactoferricin. Using oligonucleotide synthesis
to get oligonucleotides of desired peptides, and
cloned the target gene into yeast-expression
3
vectors. After the constructed bLFcin/pPICZα
B vectors were confirmed, we transformed the
recombinant vectors into Pichia pastoris by
electroporation and selected the transformants
to express the biological antibacterial peptides.
Subjects
Lactoferricin
antibacterial peptide
Pichia pastoris
yeast expression cassette
Publisher
臺北市：國立臺灣大學動物科學技術學系暨研究所
Type
report
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