Comparative biochemistry and physiology. B, Comparative biochemistry, 1992
1. D-GPDH from HeLa cells was isolated and purified. 2. Some basic kinetic constants are reported... more 1. D-GPDH from HeLa cells was isolated and purified. 2. Some basic kinetic constants are reported. 3. Sodium dodecyl polyacrylamide gel electrophoresis gave a single band with a molecular weight of approximately 36 K. 4. ATP and NADH inhibit competitively enzyme activity. 5. Comparative catalytic properties of GPDH from normal and tumor cells were effectuated.
Cyclodextrin glucanotransferase production from Bacillus clausii E16, a new bacteria isolated fro... more Cyclodextrin glucanotransferase production from Bacillus clausii E16, a new bacteria isolated from Brazilian soil samples was optimized in shake-flask cultures. A 2(4) full-factorial central composite design was performed to optimize the culture conditions, using a response surface methodology. The combined effect among the soluble starch concentration, the peptone concentration, the yeast extract concentration, and the initial pH value of the culture medium was investigated. The optimum concentrations of the components, determined by a 2(4) full-factorial central composite design, were 13.4 g/L soluble starch, 4.9 g/L peptone, 5.9 g/L yeast extract, and initial pH 10.1. Under these optimized conditions, the maximum cyclodextrin glucanotransferase activity was 5.9 U/mL after a 48-h fermentation. This yield was 68% higher than that obtained when the microorganism was cultivated in basal culture medium.
The alkalophilic bacteria Bacillus licheniformis 77-2 produces significant quantities of thermost... more The alkalophilic bacteria Bacillus licheniformis 77-2 produces significant quantities of thermostable cellulase-free xylanases. The crude xylanase was purified to apparent homogeneity by gel filtration (G-75) and ionic exchange chromatography (carboxymethyl sephadex, Q sepharose, and Mono Q), resulting in the isolation of two xylanases. The molecular masses of the enzymes were estimated to be 17 kDa (X-I) and 40 kDa (X-II),
UTILIZATION OF RESIDUAL LIQUID ORANGE FROM JUICE PROCESSING AS CULTIVA-TION MEDIUM OF PENICILLIUM... more UTILIZATION OF RESIDUAL LIQUID ORANGE FROM JUICE PROCESSING AS CULTIVA-TION MEDIUM OF PENICILLIUM CITRINUM: BIOLOGICAL DEPURATION OF THE RESI-DUE AND ENZYME PRODUCTION. Penicillium citrinum grown in orange juice processing wastes ...
Polygalacturonases production by newly isolated Monascus sp N8 and Aspergillus sp N12 strains was... more Polygalacturonases production by newly isolated Monascus sp N8 and Aspergillus sp N12 strains was carried out in solid-state fermentation using mixtures of wheat bran, sugar cane bagasse and orange bagasse as carbon sources. The maximal activity values of exo-polygalacturonases (exo-Pg) from Monascus sp and Aspergillus sp were obtained using wheat bran/sugar cane bagasse/orange bagasse mixture (6.6 U/mL) and wheat bran/orange
Wood-rotting fungi have the ability to degrade lignin by secreting ligninases, a promising enzyme... more Wood-rotting fungi have the ability to degrade lignin by secreting ligninases, a promising enzyme for degradation of environmental pollutants. Nine basidiomycete strains collected just outside the city of São José do Rio Preto, upstate São Paulo, Brazil, were evaluated for their manganese peroxidase (MnP), lignin peroxidase (LiP) and laccase production by solid-state fermentation on wheat bran.Datronia caperata SP381992,Polyporus tenuiculus SP381977
World Journal of Microbiology & Biotechnology, 2001
Five Bacillus strains isolated from decaying vegetable material were cultivated on wheat bran and... more Five Bacillus strains isolated from decaying vegetable material were cultivated on wheat bran and endo-polygalacturonases, exo-polygalacturonase and pectin lyase activities in the crude enzymatic solution obtained were determined. Highest activity was observed for all enzymes when fermentation was carried out at 28 °C, the highest activity values were obtained after 120 h of cultivation for exo-PG and after 48 h
Xylanases are enzymes of great industrial interest, mainly that it concerns to pulp and paper ind... more Xylanases are enzymes of great industrial interest, mainly that it concerns to pulp and paper industries, where they can be used as aid in bleaching process causing the reducing of added chemical. Xylanases degrade xylan and improve the access of chemicals to the lignin. In this work the xylanase produced by one newly selected bacterium, Bacillus sp called strain N.
ABSTRACT [P-B.108] Sugarcane bagasse saccharification by Myceliophthora sp F2.1.4and Aspergillus ... more ABSTRACT [P-B.108] Sugarcane bagasse saccharification by Myceliophthora sp F2.1.4and Aspergillus fumigatus M7.3 enzymatic extracts D.A. Bocchini-Martins∗, M.M.S. Moretti, M. Boscolo, R. Da Silva, E. Gomes IBILCE/UNESP, Brazil Keywords: Sugarcane bagasse; Saccharification; Myceliophthora; Aspergillus; Cellulases; Xylanases Cellulose and hemicellulose from sugarcane bagasse are a source of fermentable sugars. However, the complexity of lignocellulose represents an obstacle to sugarcane enzymatic degradation, so that pretreatments should be used to facilitate the enzymes access, improving hydrolysis. In this work, sugarcane bagasse saccharification by enzymatic extracts of two thermophilic fungi was evaluated. The enzymatic extracts from Myceliophthora sp F2.1.4 and Aspergillus fumigatus M7.3, obtained by solid state fermentation on lignocellulosic residues, were used and saccharification was performed at 50 ◦C, under 150 rpm, up to 72 h. Regarding “in natura” sugarcane bagasse, using the enzymatic extract from Myceliophthora sp F 2.1.4 (580 CMCase U/g of dry bagasse) or from A. fumigatus M7.3 (119,4 U/g of dry bagasse), 45,51 and 6,77mg of reducing sugar/g of bagasse were obtained after 48 h of hydrolysis, respectively. However, when bagasse pretreated with steam explosion was used, 80,78 and 31,8mg of reducing sugar/g of bagasse were obtained, under the same conditions, representing an increasing of 77,5 and 370% on sugar releasing, respectively. The increasing on hydrolysis time and on enzyme amount did not significantly improve saccharification. When CMCase and time of hydrolysis were fixed in 250 U/g of dry bagasse and 24 h, 57,5 and 22,8mg of reducing sugar/g of bagasse were obtained using A. fumigatus M7.3 or Myceliophthora sp F2.1.4 enzymatic extracts, respectively. Fromthese datawecan infer that the steam explosion pretreatment facilitated the enzymatic hydrolysis and that the enzymatic extract of A. fumigatus seems to be better than that from Myceliophthora on sugarcane bagasse hydrolysis. doi:10.1016/j.jbiotec.2010.08.461
A cyclomaltodextrin glucanotransferase (E.C. 2.4.1.19) from a newly isolated alkalophilic and mod... more A cyclomaltodextrin glucanotransferase (E.C. 2.4.1.19) from a newly isolated alkalophilic and moderately thermophilic Paenibacillus campinasensis strain H69-3 was purified as a homogeneous protein from culture supernatant. Cyclomaltodextrin glucanotransferase was produced during submerged fermentation at 45 degrees C and purified by gel filtration on Sephadex G50 ion exchange using a Q-Sepharose column and ion exchange using a Mono-Q column. The molecular weight of the purified enzyme was 70 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the pI was 5.3. The optimum pH for enzyme activity was 6.5, and it was stable in the pH range 6.0-11.5. The optimum temperature was 65 degrees C at pH 6.5, and it was thermally stable up to 60 degrees C without substrate during 1 h in the presence of 10 mM CaCl(2). The enzyme activity increased in the presence of Co(2+), Ba(2+), and Mn(2+). Using maltodextrin as substrate, the K(m) and K(cat) were 1.65 mg/mL and 347.9 micromol/mg x min, respectively.
Comparative biochemistry and physiology. B, Comparative biochemistry, 1992
1. D-GPDH from HeLa cells was isolated and purified. 2. Some basic kinetic constants are reported... more 1. D-GPDH from HeLa cells was isolated and purified. 2. Some basic kinetic constants are reported. 3. Sodium dodecyl polyacrylamide gel electrophoresis gave a single band with a molecular weight of approximately 36 K. 4. ATP and NADH inhibit competitively enzyme activity. 5. Comparative catalytic properties of GPDH from normal and tumor cells were effectuated.
Cyclodextrin glucanotransferase production from Bacillus clausii E16, a new bacteria isolated fro... more Cyclodextrin glucanotransferase production from Bacillus clausii E16, a new bacteria isolated from Brazilian soil samples was optimized in shake-flask cultures. A 2(4) full-factorial central composite design was performed to optimize the culture conditions, using a response surface methodology. The combined effect among the soluble starch concentration, the peptone concentration, the yeast extract concentration, and the initial pH value of the culture medium was investigated. The optimum concentrations of the components, determined by a 2(4) full-factorial central composite design, were 13.4 g/L soluble starch, 4.9 g/L peptone, 5.9 g/L yeast extract, and initial pH 10.1. Under these optimized conditions, the maximum cyclodextrin glucanotransferase activity was 5.9 U/mL after a 48-h fermentation. This yield was 68% higher than that obtained when the microorganism was cultivated in basal culture medium.
The alkalophilic bacteria Bacillus licheniformis 77-2 produces significant quantities of thermost... more The alkalophilic bacteria Bacillus licheniformis 77-2 produces significant quantities of thermostable cellulase-free xylanases. The crude xylanase was purified to apparent homogeneity by gel filtration (G-75) and ionic exchange chromatography (carboxymethyl sephadex, Q sepharose, and Mono Q), resulting in the isolation of two xylanases. The molecular masses of the enzymes were estimated to be 17 kDa (X-I) and 40 kDa (X-II),
UTILIZATION OF RESIDUAL LIQUID ORANGE FROM JUICE PROCESSING AS CULTIVA-TION MEDIUM OF PENICILLIUM... more UTILIZATION OF RESIDUAL LIQUID ORANGE FROM JUICE PROCESSING AS CULTIVA-TION MEDIUM OF PENICILLIUM CITRINUM: BIOLOGICAL DEPURATION OF THE RESI-DUE AND ENZYME PRODUCTION. Penicillium citrinum grown in orange juice processing wastes ...
Polygalacturonases production by newly isolated Monascus sp N8 and Aspergillus sp N12 strains was... more Polygalacturonases production by newly isolated Monascus sp N8 and Aspergillus sp N12 strains was carried out in solid-state fermentation using mixtures of wheat bran, sugar cane bagasse and orange bagasse as carbon sources. The maximal activity values of exo-polygalacturonases (exo-Pg) from Monascus sp and Aspergillus sp were obtained using wheat bran/sugar cane bagasse/orange bagasse mixture (6.6 U/mL) and wheat bran/orange
Wood-rotting fungi have the ability to degrade lignin by secreting ligninases, a promising enzyme... more Wood-rotting fungi have the ability to degrade lignin by secreting ligninases, a promising enzyme for degradation of environmental pollutants. Nine basidiomycete strains collected just outside the city of São José do Rio Preto, upstate São Paulo, Brazil, were evaluated for their manganese peroxidase (MnP), lignin peroxidase (LiP) and laccase production by solid-state fermentation on wheat bran.Datronia caperata SP381992,Polyporus tenuiculus SP381977
World Journal of Microbiology & Biotechnology, 2001
Five Bacillus strains isolated from decaying vegetable material were cultivated on wheat bran and... more Five Bacillus strains isolated from decaying vegetable material were cultivated on wheat bran and endo-polygalacturonases, exo-polygalacturonase and pectin lyase activities in the crude enzymatic solution obtained were determined. Highest activity was observed for all enzymes when fermentation was carried out at 28 °C, the highest activity values were obtained after 120 h of cultivation for exo-PG and after 48 h
Xylanases are enzymes of great industrial interest, mainly that it concerns to pulp and paper ind... more Xylanases are enzymes of great industrial interest, mainly that it concerns to pulp and paper industries, where they can be used as aid in bleaching process causing the reducing of added chemical. Xylanases degrade xylan and improve the access of chemicals to the lignin. In this work the xylanase produced by one newly selected bacterium, Bacillus sp called strain N.
ABSTRACT [P-B.108] Sugarcane bagasse saccharification by Myceliophthora sp F2.1.4and Aspergillus ... more ABSTRACT [P-B.108] Sugarcane bagasse saccharification by Myceliophthora sp F2.1.4and Aspergillus fumigatus M7.3 enzymatic extracts D.A. Bocchini-Martins∗, M.M.S. Moretti, M. Boscolo, R. Da Silva, E. Gomes IBILCE/UNESP, Brazil Keywords: Sugarcane bagasse; Saccharification; Myceliophthora; Aspergillus; Cellulases; Xylanases Cellulose and hemicellulose from sugarcane bagasse are a source of fermentable sugars. However, the complexity of lignocellulose represents an obstacle to sugarcane enzymatic degradation, so that pretreatments should be used to facilitate the enzymes access, improving hydrolysis. In this work, sugarcane bagasse saccharification by enzymatic extracts of two thermophilic fungi was evaluated. The enzymatic extracts from Myceliophthora sp F2.1.4 and Aspergillus fumigatus M7.3, obtained by solid state fermentation on lignocellulosic residues, were used and saccharification was performed at 50 ◦C, under 150 rpm, up to 72 h. Regarding “in natura” sugarcane bagasse, using the enzymatic extract from Myceliophthora sp F 2.1.4 (580 CMCase U/g of dry bagasse) or from A. fumigatus M7.3 (119,4 U/g of dry bagasse), 45,51 and 6,77mg of reducing sugar/g of bagasse were obtained after 48 h of hydrolysis, respectively. However, when bagasse pretreated with steam explosion was used, 80,78 and 31,8mg of reducing sugar/g of bagasse were obtained, under the same conditions, representing an increasing of 77,5 and 370% on sugar releasing, respectively. The increasing on hydrolysis time and on enzyme amount did not significantly improve saccharification. When CMCase and time of hydrolysis were fixed in 250 U/g of dry bagasse and 24 h, 57,5 and 22,8mg of reducing sugar/g of bagasse were obtained using A. fumigatus M7.3 or Myceliophthora sp F2.1.4 enzymatic extracts, respectively. Fromthese datawecan infer that the steam explosion pretreatment facilitated the enzymatic hydrolysis and that the enzymatic extract of A. fumigatus seems to be better than that from Myceliophthora on sugarcane bagasse hydrolysis. doi:10.1016/j.jbiotec.2010.08.461
A cyclomaltodextrin glucanotransferase (E.C. 2.4.1.19) from a newly isolated alkalophilic and mod... more A cyclomaltodextrin glucanotransferase (E.C. 2.4.1.19) from a newly isolated alkalophilic and moderately thermophilic Paenibacillus campinasensis strain H69-3 was purified as a homogeneous protein from culture supernatant. Cyclomaltodextrin glucanotransferase was produced during submerged fermentation at 45 degrees C and purified by gel filtration on Sephadex G50 ion exchange using a Q-Sepharose column and ion exchange using a Mono-Q column. The molecular weight of the purified enzyme was 70 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the pI was 5.3. The optimum pH for enzyme activity was 6.5, and it was stable in the pH range 6.0-11.5. The optimum temperature was 65 degrees C at pH 6.5, and it was thermally stable up to 60 degrees C without substrate during 1 h in the presence of 10 mM CaCl(2). The enzyme activity increased in the presence of Co(2+), Ba(2+), and Mn(2+). Using maltodextrin as substrate, the K(m) and K(cat) were 1.65 mg/mL and 347.9 micromol/mg x min, respectively.
Uploads
Papers by Eleni Gomes