[논문]Expression of <tex>${\\alpha}$</tex>-Galactosidase Gene from Leuconostoc mesenteroides SY1 in Lactobacillus brevis 2.14

Lee, Kang-Wook; Park, Ji-Yeong; Park, Jae-Yong; Chun, Ji-Yeon; Kim, Jeong-Hwan

[국내논문] Expression of ${\\alpha}$-Galactosidase Gene from Leuconostoc mesenteroides SY1 in Lactobacillus brevis 2.14 원문보기

Food science and biotechnology, v.17 no.5, 2008년, pp.1115 - 1118

Lee, Kang-Wook (Division of Applied Life Science (BK21 Program), Graduate School, Gyeongsang National University) , Park, Ji-Yeong (Division of Applied Life Science (BK21 Program), Graduate School, Gyeongsang National University) , Park, Jae-Yong (Division of Applied Life Science (BK21 Program), Graduate School, Gyeongsang National University) , Chun, Ji-Yeon (Department of Food Science and Technology, Sunchon National University) , Kim, Jeong-Hwan (Institute of Agriculture & Life Science, Gyeongsang National University)

Abstract ▼ AI-Helper

${\alpha}$-Galactosidase gene (aga) from Leuconostoc mesenteroides SY1 was expressed in a heterologous host, Lactobacillus brevis 2.14 using an Escherichia coli-Leuconostoc shuttle vector, pSJE. pSJEaga (pSJE carrying aga) was introduced into Lactobacillus brevis 2.14 by electroporation and transformation efficiency was $1.1{\times}10^3$ per ${\mu}g$ DNA. L. brevis transformants (TFs) showed higher ${\alpha}$-galactosidase (${\alpha}$-Gal) activities than cells containing pSJE. Transcription levels of aga in L. brevis 2.14 grown on different carbon sources (1%, w/v) were examined by slot blot analysis. Aga transcript levels and ${\alpha}$-Gal activities were higher in cells grown on melibiose, raffinose, and galactose than cells on glucose, sucrose, and fructose. Western blot result showed that L. brevis 2.14 harboring pSJEaga produced much more ${\alpha}$-Gal when grown on melibiose than on glucose.

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제안 방법

The method is based on the measurement of the absorbance at 400 nm caused by p-nitrophenol (PNP), which is released by the action of the enzyme from its specific substrate, p-nitrophenyl-α-galactopyranoside (PNPG).

이론/모형

14 were obtained as described previously (10). Protein concentrations were determined by the Bradford method (15) using a kit (500-0201EDU; Bio-Rad). α-Gal activity was measured by the method of Church et al.
Sodium dodecyl sulfate (SDS)- polyacrylamide gel electrophoresis (PAGE) was performed by the method of Laemmli (17), using a 10% gel and 5 µg of each protein sample was loaded per lane.

참고문헌 (20)

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