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Expression of porcine lactoferrin by using recombinant baculovirus in silkworm, Bombyx mori L., and its purification and characterization

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Abstract

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 μg 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.

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Acknowledgements

This work was supported by the National Basic Research Program of China (2004CB117506) and Provincial Natural Science Foundation of Zhejiang (RC01053). We sincerely thank Dr. K. Gokulamma, Department of Studies in Sericultural Science, Manasagangotri, University of Mysore, Mysore-570006, India, for critical reading of this manuscript.

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Authors and Affiliations

  1. Institute of Feed Science, The Key Laboratory of Molecular Animal Nutrition, Ministry of Education, Zhejiang University, No. 164 Qiutao North Road, Hangzhou, 310029, China

    Yizhen Wang, Guangfu Liu, Haiqing Huang & Zirong Xu

  2. Laboratory of Bioresource and Gene Engineering, College of Animal Sciences, Zhejiang University, Huajiachi Campus, Hangzhou, 310029, China

    Xiaofeng Wu & Cuiping Cao

  3. Institute of Dairy Science and Industry, Zhejiang University, Hangzhou, 310029, China

    Jianxin Liu

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  1. Yizhen Wang
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  2. Xiaofeng Wu
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  3. Guangfu Liu
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  4. Cuiping Cao
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  5. Haiqing Huang
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  6. Zirong Xu
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  7. Jianxin Liu
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Corresponding author

Correspondence to Xiaofeng Wu.

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X. Wu and G. Liu contributed equally to this work; both rank as second author.

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Wang, Y., Wu, X., Liu, G. et al. Expression of porcine lactoferrin by using recombinant baculovirus in silkworm, Bombyx mori L., and its purification and characterization. Appl Microbiol Biotechnol 69, 385–389 (2005). https://doi.org/10.1007/s00253-005-1998-y

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  • DOI: https://doi.org/10.1007/s00253-005-1998-y

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