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Title 

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

Authors 

Bong Hyun ChungDong Jin SeoSoo Wan Nam

Publisher 

Elsevier

Issue Date 

1999

Citation 

Process Biochemistry, vol. 35, no. 0, pp. 97-101

Keywords 

Human lipocortin-ISaccharomyces cerevisiaeSecretory productionGAL10 promoterOptimized expression casetteFed-batch fermentation

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.

ISSN 

0032-9592

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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