Catalytic properties of immobilized tannase produced from Aspergillus aculeatus compared with the free enzyme
نویسندگان
چکیده
منابع مشابه
Catalytical Properties of Free and Immobilized Aspergillus niger Tannase
A fungal tannase was produced, recovered, and immobilized by entrapment in calcium alginate beads. Catalytical properties of the immobilized enzyme were compared with those of the free one. Tannase was produced intracellularly by the xerophilic fungus Aspergillus niger GH1 in a submerged fermentation system. Enzyme was recovered by cell disruption and the crude extract was partially purified. T...
متن کاملCharacterization and Catalytic Activity of Free and Immobilized Lipase from Aspergillus niger: a Comparative Study
Lipase de Aspergillus niger foi imobilizada por deposição utilizando Celite e as atividades de hidrólise e esterificação, a estabilidade e a enantioseletividade das formas livre e imobilizada foram comparadas. Ambas as preparações mostraram propriedades bioquímicas similares, com atividade máxima em pH 6,0 e temperatura de 30-40 C. Não foram observadas diferenças na atividade hidrolítica em fun...
متن کاملA novel tannase from Aspergillus niger with beta-glucosidase activity.
An extracellular tannase was produced from solid-state cultures of Aspergillus niger. The enzyme was purified to homogeneity from the cell-free culture broth by preparative isoelectric focusing and by FPLC using anion-exchange and gel-filtration chromatography. SDS-PAGE analysis as well as gel localization studies of purified tannase indicated the presence of two enzyme forms, with molecular ma...
متن کاملKinetic study of free and immobilized protease from Aspergillus sp
In the present investigation partially purified alkaline protease from Aspergillus sp. As#6 and As#7 strains were entrapped in calcium alginate beads and characterized using casein as a substrate. Temperature and pH maxima of protease from As#6 strain showed no changes before and after immobilization and remained stable at 45C and pH 9, respectively. However km value was slightly shifted from 4...
متن کاملPectin methyl esterase from Aspergillus aculeatus: expression cloning in yeast and characterization of the recombinant enzyme.
Seventeen full-length cDNAs encoding pectin methyl esterase I (PME I) have been isolated from the filamentous fungus Aspergillus aculeatus by expression cloning in yeast. Yeast colonies expressing functional PME I were identified on agar plates containing highly esterified pectin, and a cDNA encoding PME I was isolated. The deduced amino acid sequence of PME I is highly similar (74% identity) t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Brazilian Journal of Chemical Engineering
سال: 2011
ISSN: 0104-6632
DOI: 10.1590/s0104-66322011000300004