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Title 

Heterologous expression and secretion of sweet potato peroxidase isoenzyme A1 in recombinant Saccharomyces cerevisiae

Authors 

Tae Hyo KimJoon Ki JungSang Soo KwakSoo Wan NamMoon Jin ChunYoung Hoon Park

Publisher 

Springer Verlag (Germany)

Issue Date 

2002

Citation 

Biotechnology Letters, vol. 24, no. 4, pp. 279-286

Keywords 

heterologous expressionprotease inhibitorsaccharomyces cerevisiaesecretionsweet potato peroxidaseisoenzymeperoxidasegene expressionpotatoprotein expression

Abstract 

A vector system has been developed to express isoenzyme A1 of sweet potato peroxidase (POD) and was introduced into Saccharomyces cerevisiae. The system contains the signal sequence of Aspergillus oryzae α-amylase to facilitate the extracellular secretion of peroxidase under the control of constitutive glyceraldehyde-3-phosphate dehydrogenase (GPD) promoter. In a batch culture using YNBDCA medium (yeast nitrogen base without amino acids 6.7 g l-1, Casamino acids 5 g l-1 and glucose 20 g l-1), the recombinant strain expressed the swpa1 gene giving a secretion yield of POD activity of ca. 90% of total expressed peroxidase. Supplementation with PMSF (0.05 mM) and Casamino acids (5 g/50 ml) increased extracellular POD activity to nearly 10 kU ml-1, equivalent to 1.5 kU g-1 cell dry wt. This is 9 fold higher than that obtained in medium without PMSF. From SDS-PAGE and native-PAGE analyses POD has an Mr of 53 kDa.

ISSN 

0141-5492

Link 

http://dx.doi.org/10.1023/A:1014053807643

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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