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RISS 인기검색어
- 검색키워드
- 저자 : Luis Henrique Souza Guimarães (검색결과 3 건)
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Biochemical Properties of an Extracellular Trehalase from Malbranchea pulchella var. Sulfurea
Marita Gimenez Pereira,Luis Henrique Souza Guimarães,Rosa Prazeres Melo Furriel,Maria de Lourdes,Hector Francisco Terenzi,Joao Atilio Jorge 한국미생물학회 2011 The journal of microbiology Vol.49 No.5
The thermophilic fungus Malbranchea pulchella var. sulfurea produced good amounts of extracellular trehalase activity when grown for long periods on starch, maltose or glucose as the main carbon source. Studies with young cultures suggested that the main role of the extracellular acid trehalase is utilizing trehalose as a carbon source. The specific activity of the purified enzyme in the presence of manganese (680 U/mg protein) was comparable to that of other thermophilic fungi enzymes, but many times higher than the values reported for trehalases from other microbial sources. The apparent molecular mass of the native enzyme was estimated to be 104 kDa by gel filtration and 52 kDa by SDS-PAGE, suggesting that the enzyme was composed by two subunits. The carbohydrate content of the purified enzyme was estimated to be 19% and the pI was 3.5. The optimum pH and temperature were 5.0-5.5 and 55°C, respectively. The purified enzyme was stimulated by manganese and inhibited by calcium ions, and insensitive to ATP and ADP, and 1 mM silver ions. The apparent K_M values for trehalose hydrolysis by the purified enzyme in the absence and presence of manganese chloride were 2.70±0.29 and 2.58±0.13 mM, respectively. Manganese ions affected only the apparent V_(max), increasing the catalytic efficiency value by 9.2-fold. The results reported herein indicate that Malbranchea pulchella produces a trehalase with mixed biochemical properties, different from the conventional acid and neutral enzymes and also from trehalases from other thermophilic fungi.
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Effect of Glycosylation on the Biochemical Properties of β-Xylosidases from Aspergillus versicolor
Alexandre Favarin Somera,Marita Gimenez Pereira,Luis Henrique Souza Guimarães,Maria de L.T. de M. Polizeli,Héctor Francisco Terenzi,Rosa Prazeres Melo Furriel,João Atílio Jorge 한국미생물학회 2009 The journal of microbiology Vol.47 No.3
Aspergillus versicolor grown on xylan or xylose produces two β-xylosidases with differences in biochemical properties and degree of glycosylation. We investigated the alterations in the biochemical properties of these β-xylosidases after deglycosylation with Endo-H or PNGase F. After deglycosylation, both enzymes migrated faster in PAGE or SDS-PAGE exhibiting the same Rf. Temperature optimum of xylan-induced and xylose-induced β-xylosidases was 45°C and 40°C, respectively, and 35°C after deglycosylation. The xylan- induced enzyme was more active at acidic pH. After deglycosylation, both enzymes had the same pH optimum of 6.0. Thermal resistance at 55°C showed half-life of 15 min and 9 min for xylose- and xylan-induced enzymes, respectively. After deglycosylation, both enzymes exhibited half-lives of 7.5 min. Native enzymes exhibited different responses to ions, while deglycosylated enzymes exhibited identical responses. Limited proteolysis yielded similar polypeptide profiles for the deglycosylated enzymes, suggesting a common polypeptide core with differential glycosylation apparently responsible for their biochemical and biophysical differences.
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Heloísa Bressan Gonçalves,João Atílio Jorge,Luis Henrique Souza Guimarães 한국식품과학회 2015 Food Science and Biotechnology Vol.24 No.4
The extracellular β-D-fructofuranosidase from Fusarium graminearum was immobilized using hydrophilic cotton, filter paper, multipurpose cloth, sugar cane bagasse, string, or gauze as alternative cellulosic supports, or with cyanogen bromide agarose. All derivatives (support+enzyme) showed high capacity for reuse (up to 23 times). The derivatives obtained with multipurpose cloth and string were stable at 60℃ maintaining 80% of their activity for more than 120 min. The filter paper derivative had a halflife (T50) of 27 min at 70℃. When tested for their pH stability (3.0-9.0), all derivatives were more stable than the free enzyme, especially the cotton derivative. The sugarcane bagasse, string, and filter paper derivatives could efficiently produce fructooligosaccharides (FOS) using sucrose as substrate. According to the retention of enzymatic activity, reuse and stabilities, the filter paper and string were the best alternative supports for β-D-fructofuranosidase immobilization, allowing enzyme stabilization and production of FOS.
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