Expression of porcine lactoferrin by using recombinant baculovirus in silkworm, Bombyx mori L., and its purification and characterization.
Lactoferrin is a multifunctional glycoprotein that is present in several mucosal secretions. In this study, we exploited the silkworm, Bombyx mori, as host for the recombinant baculovirus harboring the porcine lactoferrin (PLF) gene to produce the recombinant PLF (rPLF). Around 205 mug of rPLF was purified from a single silkworm pupa infected by the virus and the rPLF was proved to be biologically active. This method established in our study will pave the way for efficient industrial production of rPLF on a large scale for further utilization of this protein as a feed additive in the future.
Wang
Yizhen
Y
Institute of Feed Science, The Key Laboratory of Molecular Animal Nutrition, Ministry of Education, Zhejiang University, No. 164 Qiutao North Road, Hangzhou 310029, China.
Wu
Xiaofeng
X
Liu
Guangfu
G
Cao
Cuiping
C
Huang
Haiqing
H
Xu
Zirong
Z
Liu
Jianxin
J
D000818:Animals; D016367:Baculoviridae / Q000235:genetics* / Q000502:physiology; D012831:Bombyx / Q000821:virology*; D002478:Cells, Cultured; D004926:Escherichia coli / Q000187:drug effects; D007218:Industrial Microbiology / Q000379:methods; D007781:Lactoferrin / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D018411:Spodoptera / Q000821:virology; D013552:Swine
D011994:Recombinant Proteins; D007781:Lactoferrin