Consulta: creatorFacets:"Ahmad,Waqar"
Registros recuperados: 2
Data/hora: 09/06/2024 11:59:23

Medium optimization of protease production by Brevibacterium linens DSM 20158, using statistical approach
Provedor de dados: 58
Autores: Shabbiri,Khadija; Adnan,Ahmad; Jamil,Sania; Ahmad,Waqar; Noor,Bushra; Rafique,H.M.
Various cultivation parameters were optimized for the production of extra cellular protease by Brevibacterium linens DSM 20158 grown in solid state fermentation conditions using statistical approach. The cultivation variables were screened by the Plackett-Burman design and four significant variables (soybean meal, wheat bran, (NH4)2SO4 and inoculum size were further optimized via central composite design (CCD) using a response surface methodological approach. Using the optimal factors (soybean meal 12.0g, wheat bran 8.50g, (NH4)2SO4) 0.45g and inoculum size 3.50%), the rate of protease production was found to be twofold higher in the optimized medium as compared to the unoptimized reference medium.
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Brevibacterium linens; Protease; Solid-state fermentation; Plackett-Burman Design; Central Composite Design (CCD).
Ano: 2012
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000300031

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