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Concentration, characterization and application of lipases from Sporidiobolus pararoseus strain BJM
Smaniotto,Alessandra; Skovronski,Aline; Rigo,Elisandra; Tsai,Siu Mui; Durrer,Ademir; Foltran,Lillian Liva; Paroul,Natália; Luccio,Marco Di; Oliveira,J. Vladimir; Oliveira,Débora de; Treichel,Helen.
Lipases produced by a newly isolated Sporidiobolus pararoseus strain have potential catalytic ability for esterification reactions. After production, the enzymatic extracts (conventional crude and precipitated, 'CC' and 'CP', and industrial crude and precipitated, 'IC' e 'IP') were partially characterized. The enzymes presented, in general, higher specificity for short chain alcohols and fatty acids. The precipitated extract showed a good thermal stability, higher than that for crude enzymatic extracts. The 'CC' and 'CP' enzymes presented high activities after exposure to pH 6.5 and 40 ºC. On the other hand, the 'IC' and 'IP' extracts kept their activities in a wide range of pH memory but presented preference for higher reaction temperatures. Preliminary...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Sporidiobolus pararoseus; 'synthetic lipase'; Submerged fermentation; Enzyme characterization.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822014000100043
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Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates Electron. J. Biotechnol.
Fanchini Terrasan,César Rafael; Guisan,José Manuel; Cano Carmona,Eleonora.
Background: Xylanases and β-D-xylosidases are the most important enzymes responsible for the degradation of xylan, the second main constituent of plant cell walls. Results: In this study, the main extracellular xylanase (XYL I) and p-xylosidase (BXYL I) from the fungus Penicillium janczewskii were purified, characterized and applied for the hydrolysis of different substrates. Their molecular weights under denaturing and non-denaturing conditions were, respectively, 30.4 and 23.6 kDa for XYL I, and 100 and 200 kDa for BXYL I, indicating that the latter is homodimeric. XYL I is highly glycosylated (78%) with optimal activity in pH 6.0 at 65°C, while BXYL I presented lower sugar content (10.5%) and optimal activity in pH 5.0 at 75°C. The half-lives...
Tipo: Journal article Palavras-chave: Xylanolytic enzymes; Enzyme characterization; Enzyme purification; Xylan hydrolysis; Xylooligosaccharides hydrolysis.
Ano: 2016 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000500006
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