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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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Cesar Vanderlei Nascimento,Flávio Henrique Moreira Souza,Douglas Chodi Masui,Francisco Assis Leone,Rosane Marina Peralta,João Atílio Jorge,Rosa Prazeres Melo Furriel 한국미생물학회 2010 The journal of microbiology Vol.48 No.1
The effect of several carbon sources on the production of mycelial-bound β-glucosidase by Humicola grisea var. thermoidea in submerged fermentation was investigated. Maximum production occurred when cellulose was present in the culture medium, but higher specific activities were achieved with cellobiose or sugarcane bagasse. Xylose or glucose (1%) in the reaction medium stimulated β-glucosidase activity by about 2-fold in crude extracts from mycelia grown in sugarcane bagasse. The enzyme was purified by ammonium sulfate precipitation, followed by Sephadex G-200 and DEAE-cellulose chromatography, showing a single band in PAGE and SDS-PAGE. The β-glucosidase had a carbohydrate content of 43% and showed apparent molecular masses of 57 and 60 kDa, as estimated by SDS-PAGE and gel filtration, respectively. The optimal pH and temperature were 6.0 and 50°C, respectively. The purified enzyme was thermostable up to 60 min in water at 55°C and showed half-lives of 7 and 14 min when incubated in the absence or presence of 50 mM glucose, respectively, at 60°C. The enzyme hydrolyzed p-nitrophenyl-β-D-glucopyranoside, p-nitrophenyl-β-Dgalactopyranoside,p-nitrophenyl-β-D-fucopyranoside, p-nitrophenyl-β-D-xylopyranoside, o-nitrophenyl-β-Dgalactopyranoside,lactose, and cellobiose. The best synthetic and natural substrates were p-nitrophenyl-β-Dfucopyranoside and cellobiose, respectively. Purified enzyme activity was stimulated up to 2-fold by glucose or xylose at concentrations from 25 to 200 mM. The addition of purified or crude β-glucosidase to a reaction medium containing Trichoderma reesei cellulases increased the saccharification of sugarcane bagasse by about 50%. These findings suggest that H. grisea var. thermoidea β-glucosidase has a potential for biotechnological applications in the bioconversion of lignocellulosic materials.
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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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