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Isolation of natural inhibitors of papain obtained from Carica papaya latex BABT
Monti,Rubens; Contiero,Jonas; Goulart,Antonio José.
Studies were carried out to natural papain inhibitor from papaya latex. Fresh latex from green fruits of Carica papaya was collected and immediately transported in ice bath to the lab, from which three fractions with inhibitor effect of esterase papain activity were isolated by latex dialysis, Sephadex G-25 gel filtration and ionic exchange chromatography in SP-Sephadex C-25. The isolated fractions, identified as inhibitors I and II, showed a negative reaction with ninhydrin; however, the fraction identified as P-III showed positive reaction with ninhydrin. Kinetics data showed non-competitive inhibition (inhibitor I) and uncompetitive (inhibitors II and P-III).
Tipo: Info:eu-repo/semantics/article Palavras-chave: Esterase activity; Natural papain inhibitor; Protease inhibitor.
Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132004000500010
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Partial purification and properties of cellulase-free alkaline xylanase produced by Rhizopus stolonifer in solid-state fermentation BABT
Goulart,Antonio José; Carmona,Eleonora Cano; Monti,Rubens.
Rhizopus stolonifer was cultivated in wheat bran to produce a cellulase-free alkaline xylanase. The purified enzyme obtained after molecular exclusion chromatography in Sephacryl S-200 HR showed optimum temperature as 45º C and hydrolysis pHs optima as pH 6.0 and 9.0. Xylanase presented higher Vmax at pH 9.0 (0.87 µmol/mg protein) than at pH 6.0 and minor Km at pH 6.0 (7.42 mg/mL) than at pH 9.0.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Alkaline xylanase; Rhizopus stolonifer; Solid-state fermentation.
Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132005000300001
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Cyclodextrin glycosyltransferase production by new Bacillus sp. strains isolated from brazilian soil BJM
Menocci,Vivian; Goulart,Antonio José; Adalberto,Paulo Roberto; Tavano,Olga Luisa; Marques,Daniela Parreira; Contiero,Jonas; Monti,Rubens.
Three strains of Bacillus sp. (BACRP, BACNC-1 and BACAR) were isolated from soil adhered to cassava husk. CGTase specific activity for the three isolated strains was higher when cultivated at 40ºC. Potato starch, cassava starch, maltodextrin and glucose were used as carbon source and growth temperatures varied from 25 to 55ºC. The three isolates presented higher CGTase specific activity when cultivated with potato starch at 40ºC. Isolated BACRP and BACAR presented specific activity of 4.0x10-3 and 2.2x10-3 U/mg prot at pH 7.0, respectively, when cultivated in mediums added with NaCl 2%; at pH 10,0 their activities were of 3.4x10-3 and 3.0x10-3 U/mg prot, respectively, in the same concentration of NaCl. On the other hand, the isolated BACNC-1 presented...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Cyclodextrin glycosyltransferase; CGTase production.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000400016
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Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its properties BJM
Bonilha,Paulo Roberto Martins; Menocci,Vivian; Goulart,Antonio José; Polizeli,Maria de Lourdes Teixeira de Moraes; Monti,Rubens.
Cyclodextrin glycosyltransferase (EC 2.4.1.19) is an enzyme that produces cyclodextrins from starch via an intramolecular transglycosylation reaction. An alkalophilic Bacillus strain, isolated from cassava peels, was identified as Bacillus licheniformis. CGTase production by this strain was better when potato starch was used as carbon source, followed by cassava starch and amylopectin. Glucose and amylose, on the other hand, acted as synthesis repressors. When the cultivation was supplemented with sodium ions and had the pH adjusted between 6.0 and 9.0, the microorganism maintained the growth and enzyme production capacity. This data is interesting because it contradicts the concept that alkalophilic microorganisms do not grow in this pH range. After...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Cyclodextrin glycosyltransferase; CGTase production; Bacilluslicheniformis; Bacillus beta-CD.
Ano: 2006 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822006000300022
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