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Stability and Growth Characteristics of GFPuv- Labeled Cronobacter sakazakii Isolated from Foods
Siti Nurjanah,Ratih Dewanti-Hariyadi,Sri Estuningsih,Maggy Thenawidjaja Suhartono 한국식품과학회 2014 Food Science and Biotechnology Vol.23 No.5
Stability of ultraviolet green fluorescent protein(GFPuv)-labeled Cronobacter sakazakii and C. muytjensiiisolated from foods and the effects of the plasmid GFPuv(pGFPuv) on growth were analyzed. PCR analysis andmicroscopic observation showed that C. sakazakii and C. muytjensii isolates took up the plasmid into cells andexpressed the GFPuv gene. All Cronobacter transformantsmaintained this plasmid after frozen storage and 2consecutive subcultures. The C. sakazakii FWHd16transformant was the most stable, while the C. muytjensiiFWHd11 transformant was the least stable. All transformantsshowed nearly identical growth curves during lag, log andstationary phases, compared to wild type parental isolates. The maximum bacterial growth rates (μmax) of thetransformants and parents were similar, indicating that thepresence of pGFPuv in transformants did not affect cellgrowth. Stable GFPuv-labeled Cronobacter has potentialfor use in tracking bacterial behavior during food handlingand drying.
Afifah, Diana Nur,Sulchan, Muhammad,Syah, Dahrul,Yanti, Yanti,Suhartono, Maggy Thenawidjaja,Kim, Jeong Hwan The Korean Society of Food Science and Nutrition 2014 Preventive Nutrition and Food Science Vol.19 No.3
Bacillus pumilus 2.g isolated from gembus, an Indonesian fermented soybean cake, secretes several proteases that have strong fibrinolytic activities. A fibrinolytic enzyme with an apparent molecular weight of 20 kDa was purified from the culture supernatant of B. pumilus 2.g by sequential application of ammonium sulfate precipitation, ion-exchange chromatography, and hydrophobic chromatography. The partially purified enzyme was stable between pH 5 and pH 9 and temperature of less than $60^{\circ}C$. Fibrinolytic activity was increased by 5 mM $MgCl_2$ and 5 mM $CaCl_2$ but inhibited by 1 mM phenylmethylsulfonyl fluoride (PMSF), 1 mM sodium dodecyl sulfate (SDS), and 1 mM ethylenediaminetetraacetic acid (EDTA). The partially purified enzyme quickly degraded the ${\alpha}$ and ${\beta}$ chains of fibrinogen but was unable to degrade the ${\gamma}$ chain.
Diana Nur Afifah,Muhammad Sulchan,Dahrul Syah,Yanti,Maggy Thenawidjaja Suhartono,김정환 한국식품영양과학회 2014 Preventive Nutrition and Food Science Vol.19 No.3
Bacillus pumilus 2.g isolated from gembus, an Indonesian fermented soybean cake, secretes several proteases that have strong fibrinolytic activities. A fibrinolytic enzyme with an apparent molecular weight of 20 kDa was purified from the culture supernatant of B. pumilus 2.g by sequential application of ammonium sulfate precipitation, ion-exchange chromatography, and hydrophobic chromatography. The partially purified enzyme was stable between pH 5 and pH 9 and temperature of less than 60oC. Fibrinolytic activity was increased by 5 mM MgCl2 and 5 mM CaCl2 but inhibited by 1 mM phenylmethylsulfonyl fluoride (PMSF), 1 mM sodium dodecyl sulfate (SDS), and 1 mM ethylenediaminetetraacetic acid (EDTA). The partially purified enzyme quickly degrades the α and β chains of fibrinogen but cannot degrade the γ chain.
Diana Nur Afifah,Muhammad Sulchan,Dahrul Syah,Yanti,Maggy Thenawidjaja Suhartono,Jeong Hwan Kim 한국식품영양과학회 2014 Preventive Nutrition and Food Science Vol.19 No.3
Bacillus pumilus 2.g isolated from gembus, an Indonesian fermented soybean cake, secretes several proteases that have strong fibrinolytic activities. A fibrinolytic enzyme with an apparent molecular weight of 20 kDa was purified from the culture supernatant of B. pumilus 2.g by sequential application of ammonium sulfate precipitation, ion-exchange chromatography, and hydrophobic chromatography. The partially purified enzyme was stable between pH 5 and pH 9 and temperature of less than 60 ℃. Fibrinolytic activity was increased by 5 mM MgCl2 and 5 mM CaCl2 but inhibited by 1 mM phenylmethylsulfonyl fluoride (PMSF), 1 mM sodium dodecyl sulfate (SDS), and 1 mM ethylenediaminetetraacetic acid (EDTA). The partially purified enzyme quickly degraded the α and β chains of fibrinogen but was unable to degrade the γ hain.