Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Jaya Ram Simkhada"'
Autor:
Yun Hee Choi, Seung Sik Cho, Jaya Ram Simkhada, Md Saifur Rahman, Yoon Seok Choi, Chun Sung Kim, Jin Cheol Yoo
Publikováno v:
PLoS ONE, Vol 12, Iss 5, p e0176971 (2017)
CSP32 has stable characteristics and may find bio-industrial and therapeutic applications.
Externí odkaz:
https://doaj.org/article/9638933ef4454334baf0ee007ac8f5e4
Autor:
Yun Hee Choi, Jin Cheol Yoo, Hong Seop Moon, Chi Nam Seong, Seung Sik Cho, Hyo-Jeong Lee, Jaya Ram Simkhada
Publikováno v:
African Journal of Biotechnology; Vol 12, No 17 (2013)
An antimicrobial compound, highly effective against multidrug-resistant (MDR) bacteria, purified from a Streptomyces strain was identified as manumycin. The minimal inhibitory concentrations (MICs) of manumycin against 8 different strains of methicil
Publikováno v:
International Journal of Antimicrobial Agents. 40:80-83
In an attempt to isolate effective antimicrobial peptides (AMPs) from a microbial source for the treatment of multidrug-resistant (MDR) bacteria, BCP61 was purified from Bacillus sp. CS61 newly isolated from the traditional fermented food kimchi. BCP
Publikováno v:
Process Biochemistry. 47:635-642
The enzymatic route for biodiesel production has been noted to be cost ineffective due to the high cost of biocatalysts. Reusing the biocatalyst for successive transesterification cycles is a potential solution to address such cost inefficiency. Howe
Autor:
Da Jeong Park, Jung Wan Ha, Jin Cheol Yoo, Seung Sik Cho, Jaya Ram Simkhada, Poonam Mander, Yun Hee Choi
Publikováno v:
Biotechnology and Bioprocess Engineering. 17:67-75
In an effort to identify a microbial lipase that can catalyze transesterification reactions used in biodiesel production, an organic solvent-tolerant lipase was purified from Streptomyces sp. CS268. The molecular weight of the purified lipase was est
Publikováno v:
Process Biochemistry. 46:1449-1455
A proteolytic enzyme with fibrinolytic activity (FES624) was purified from recently isolated Streptomyces sp. CS624. SDS-PAGE of the enzyme showed a single polypeptide chain with molecular weight of 18 kDa, which is the lowest among the so far report
Autor:
Seung Wook Kim, Chi Nam Seong, Seung Sik Cho, Jaya Ram Simkhada, Hah Young Yoo, Don Hee Park, Jin Cheol Yoo
Publikováno v:
Bioresource Technology. 102:6104-6111
With the aim of isolating a biocatalyst able to catalyze biodiesel production from microbial source, Ralstonia sp. CS274 was isolated and a lipase from the strain (RL74) was purified. Molecular weight of RL74 was estimated to be 28,000 Da by SDS-PAGE
Autor:
Jae Kyung Sohng, Seung Sik Cho, Jin Cheol Yoo, Jaya Ram Simkhada, Hei Chan Lee, Si Wouk Kim, Hong Seok Choi
Publikováno v:
Biotechnology and Bioprocess Engineering. 15:595-602
A phospholipase D (PLD628), constitutively secreted by Streptomyces sp. CS628, was purified by ion exchange with CM Trisacryl and gel filtration with Sepharose CL-6B. The enzyme production was highest with peptone and starch as nitrogen and carbon so
Publikováno v:
Process Biochemistry. 45:88-93
A fibrinolytic protease (FP84) was purified from Streptomyces sp. CS684, with the aim of isolating economically viable enzyme from a microbial source. SDS-PAGE and fibrin zymography of the purified enzyme showed a single protein band of approximately
A novel Ca2+-dependent phospholipase D from Streptomyces tendae, possessing only hydrolytic activity
Autor:
Jin Cheol Yoo, Jaya Ram Simkhada, Jae Kyung Sohng, Hei Chan Lee, Poonam Mander, Sung Ju Park, Seung Sik Cho, Hong Seok Choi
Publikováno v:
Archives of Pharmacal Research. 32:1461-1467
An extracellular phospholipase D (PLD(St)) was purified from Streptomyces tendae by two successive chromatographic steps on Sepharose CL-6B and DEAE-Sepharose CL-6B. Molecular weight of the PLD(St) was estimated to be approximately 43 kDa by sodium d