High-level secretory production of recombinant human lipocortin-I by saccharomyces cerevisiae

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Title
High-level secretory production of recombinant human lipocortin-I by saccharomyces cerevisiae
Author(s)
Bong Hyun Chung; Dong Jin Seo; Soo Wan Nam
Bibliographic Citation
Process Biochemistry, vol. 35, pp. 97-101
Publication Year
1999
Abstract
Human lipocortin-I was very efficiently produced as a secretory product by Saccharomyces cerevisiae harbouring an optimized expression casette containing the GAL10 promoter, inulinase signal sequence and the lipocortin-I terminator. To overproduce lipocortin-I, a fed-batch fermentation was performed. The feed medium contained only glucose as sole carbon source and was first fed for cell growth. A mixture of glucose and galactose was then fed for gene induction in parallel with cell growth. During the gene induction period, a significant amount of lipocortin-I accumulated in the culture medium. However, about 45% of the secreted lipocortin-I existed in a proteolytically-cleaved form, cleaved after the basic amino acid Lys26. At the end of the culture, the concentration of total extracellular lipocortin-I (intact form + cleaved form) was about 2.1 g/l, accounting for more than 80% of the total extracellular protein.
Keyword
Human lipocortin-ISaccharomyces cerevisiaeSecretory productionGAL10 promoterOptimized expression casetteFed-batch fermentation
ISSN
0032-9592
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/S0032-9592(99)00038-2
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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