Consulta: creatorFacets:"Syed,Quratulain"
Registros recuperados: 2
Data/hora: 09/06/2024 11:48:27

Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae
Provedor de dados: 52
Autores: Mushtaq,Zareena; Irfan,Muhammad; Nadeem,Muhammad; Naz,Mammona; Syed,Quratulain.
In this study, extracellular alkaline protease was produced from Rhizopus oryzae in submerged fermentation using dairy waste (whey) as a substrate. Fermentation kinetics was studied and various parameters were optimized. The strain produced maximum protease at initial medium pH of 6.0 medium depth of 26 mm, inoculum size of 2% at incubation temperature of 35ºC for 168 h of fermentation. Alkaline protease was purified to homogeneity by ammonium sulphate fractionation followed by sephadex G-100 chromatography. The molecular mass of alkaline protease was 69 kDa determined by 10% SDS-PAGE. The optimum pH and temperature of alkaline protease was 9.0 and 40ºC, respectively. Metal profile of the enzyme showed that the enzyme was non-metallic in nature. The Km ,...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Kinetics; Purification; Characterization; Protease; Detergent stability; Rhizopus oryzae.
Ano: 2015
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000200175

Isolation and purification of complex II from proteus mirabilis strain ATCC 29245
Provedor de dados: 58
Autores: Shabbiri,Khadija; Ahmad,Waqar; Syed,Quratulain; Adnan,Ahmad.
A respiratory complex was isolated from plasma membrane of pathogenic Proteus mirabilis strain ATCC 29245. It was identified as complex II consisting of succinate:quinone oxidoreductase (EC 1.3.5.1) containing single heme b. The complex II was purified by ion-exchange chromatography and gel filtration. The molecular weight of purified complex was 116.5 kDa and it was composed of three subunits with molecular weights of 19 kDa, 29 kDa and 68.5 kDa. The complex II contained 9.5 nmoles of cytochrome b per mg protein. Heme staining indicated that the 19 kDa subunit was cytochrome b. Its reduced form showed absorptions peaks at 557.0, 524.8 and 424.4 nm. The α-band was shifted from 557.0 nm to 556.8 nm in pyridine ferrohemochrome spectrum. The succinate:...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Proteus mirabilis; Complex II; Cytochrome b.
Ano: 2010
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822010000300032