Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/62029
標題: Functional secretion of a type 1 antifreeze protein analogue by optimization of promoter, signal peptide, prosequence, and terminator in Lactococcus lactis
作者: Yeh, C.M.
葉娟美
Huang, X.H.
Sue, C.W.
關鍵字: type 1 antifreeze protein analogue;extracellular production;Lactococcus lactis;bacillus-subtilis;heterologous protein;lactobacillus-acidophilus;expression system;escherichia-coli;cloning;gene;bacteria;sequence;charge
Project: Journal of Agricultural and Food Chemistry
期刊/報告no:: Journal of Agricultural and Food Chemistry, Volume 56, Issue 18, Page(s) 8442-8450.
摘要: 
Lactococcus lactis is a food-grade microorganism of major commercial importance. Antifreeze protein is a potent cryogenic protection agent for the cryopreservation of food and pharmaceutical materials. In this study, extracellular expression of a novel recombinant type 1 antifreeze protein analogue (rAFP) in L. lactis was optimized. An efficient SlpA promoter (P-SlpA) was fused to various signal peptides (SPs) and propeptide sequences to examine the extracellular expression levels of rAFP. An efficient signal peptide, SPsacB, fused to prosequence AE, enabled higher extracellular rAFP production; use of the S-lpA terminator (Ter(SlpA)) was a further improvement. The extracellularly expressed rAFP successfully inhibited ice recrystallization and is thus potentially applicable for cryogenic preservation.
URI: http://hdl.handle.net/11455/62029
ISSN: 0021-8561
DOI: 10.1021/jf801580s
Appears in Collections:食品暨應用生物科技學系

Show full item record
 

Google ScholarTM

Check

Altmetric

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.