Can artisanal "Coalho" cheese from Northeastern Brazil be used as a functional food?

Brazilian artisanal "Coalho" cheeses from six Northeast towns were investigated as a functional food based on their peptide profiles and antioxidant, zinc-binding and antimicrobial activities. The peptides (WSP) from "Coalho" cheese showed high antioxidant activity, the best value of TEAC being 2223±10.10µM, which means 91.1±0.43% oxidative inhibition and peptide concentration for IC(50) of 7mg/mL (21µg of peptides) for sample from the town of Correntes. The smallest TEAC value (1896±17µM), which means 75.9±0.7% oxidative inhibition and IC(50) of 10.5mg/mL (31.5µg of peptide), was obtained for samples from the town of São Bento do Una. The zinc-binding activities were: Arcoverde (72.21±0.24%) Cachoeirinha (75.02±0.02%), Capoeiras (61.78±0.65%), Correntes (75.47±0.5%), São Bento do Una (75.41±0.15%), and Venturosa (74.36±0.04%). The WSP extracts showed antimicrobial activity against Enterococcus faecalis, Bacillus subtilis, Escherichia coli and Pseudomonas aeruginosa. All the results obtained suggest that "Coalho" cheese has potential as a functional food.

Covalent immobilization of invertase on polyurethane, plast-film and ferromagnetic Dacron.

Invertase was covalently immobilized on polyurethane (PU), inox plate covered with plast-film layer and ferromagnetic azide-Dacron. The immobilization processes, physico-chemical parameters and a model for coupling reactions were studied. The preliminary studies for selection of the support showed that the best activity was obtained for PU treated with HCl, polyethylenimine and glutaraldehyde (156.7+/-4.9 U/g support). All plast-film-invertase derivatives did not show activity and the Dacron-invertase derivative showed an activity of 105.39 U/g support. The invertase immobilized in presence of substrate (10% w/v sucrose) was the most efficient (832.74+/-1.48 U/g support). The optimal pH was shifted from 4.5 (free enzyme) to 5.0 (immobilized derivative) and optimal temperature was not affected. Activation energy values of free enzyme, Dacron-invertase and PU-invertase were 32.4+/-0.34 kJ/mol, 33.4+/-0.36 kJ/mol and 44.0+/-0.67 kJ/mol, respectively. The PU-invertase could be used over 2 months without considerable activity loss (68.5% activity retention) and retained 12.6% (287.97+/-27.9U/g support) of the activity after five cycles.

Immobilization of Candida rugosa lipase on magnetized Dacron: kinetic study.

Candida rugosa lipase has been covalently immobilized on ferromagnetic azide polyethyleneterepthalate (Dacron) with specific activity retention of 16% for 4-nitrophenyl palmitate and 24% for hydrolysis of triolein in hexane. The immobilized enzyme was more thermal stable than the soluble one, retaining 78.8% of the activity after 1 h at 60 degrees C. Also, this immobilized derivative was stable at the storage at 4 degrees C. It has been used 5 cycles for pNPP hydrolysis without loss of activity. Soluble and immobilized Candida rugosa lipase showed a Michaelian behavior for fatty acid 4-nitrophenyl esters and different apparent K(M) values: 0.110 mM and 0.124 mM (4-nitrophenyl palmitate - C16); 0.193 mM and 0.235 mM (4-nitrophenyl laurate - C12) and 0.206 mM and 0.119 mM (4-nitrophenyl butyrate - C4), respectively. The immobilized lipase was more efficient for catalyzing the hydrolysis of 4-nitrophenyl esters with short chain length fatty acid (4-NPB - C4) than soluble enzyme. The ferromagnetic Dacron-lipase derivative was able to catalyze the synthesis of triolein from glycerol and oleic acid with 50% of conversion after 72 h at 40 degrees C.

Determinação de atividade antimicrobiana de extratos de plantas de uso popular como antiflamatório

Antimicrobial activities of “babaçu” (Orbignya martiana), “cardo santo” (Argemone mexicana), “mentrasto” (Ageratum conyzoides), “cavalinha” (Equisetum yeamalis) and “terramicina” (Alternanthera brasiliana), used by Brazilian population as antiinflamatory medicine, were studied on Staphylococcus aureus. The freezer dried hydroalcoholic extracts solutions were tested for 7 strains of Staphylococcus aureus, which two of those are methicillin resistant (MRSA). The diffusion method on agar-agar, using holes technique, with tetracycline chlorydrate as standard. “Babaçu”, “cardo santo” and “terramicina” showed antimicrobial activity, within of those “terramicina” inhibited 6 strains, presenting zone inhibition of 22 mm compared to standard antibiotic (34 mm), except the seventh strain which was also tetracycline resistant.

Production of lipase free of citrinin by Penicillium citrinum.

Lipase (Glycerol ester hydrolase E.G. 3.1.1.3) from a Brazilian strain of Penicillium citrinum free of the mycotoxin citrinin has been investigated. Citrinin production was inhibited by using culture medium containing olive oil, soybean oil and corn oil as carbon sources. Potassium concentration and pH play an important role in citrinin production. Potassium concentration lower than 30 mM and pH below 4.5 inhibited the mycotoxin production. P. citrinum produced lipase free of extraneous proteins and citrinin when cultured using, as nitrogen source, ammonium sulphate (lipase activity of 7.88 U/mg) and yeast extract (lipase activity of 4.95 U/mg) with olive oil as carbon source. This data is relevant to the larger scale production of lipases for food technology applications, from Penicillium citrinum.

Lipase from a Brazilian strain of Penicillium citrinum.

A lipases (glycerol ester hydrolases E. C. 3.1.1.3) from a brazilian strain of Penicillium citrinum has been investigated. When the microorganism was cultured in the simple medium (1.0% olive oil and 0.5% yeast extract), using olive oil in as carbon source in the inocula, the enzyme extracted showed maximum activity (409 IU/mL). In addition, decrease of yeast extract concentration also reduces the lipase activity. Nevertheless, when yeast extract was replaced by ammonium sulfate, no activity was detected. Purification by precipitation with ammonium sulfate showed best activity in the 40-60% fraction. The optimum temperature for enzyme activity was found in the range of 34-37 degrees C. However, after 30 min at 60 degrees C, the enzyme was completely inactivated. The enzyme showed optimum at pH 8.0. The dried concentrated fraction (after dialysis and lyophilization) maintained its lipase activity at room temperature (28 degrees C) for 8 mo. This result in lipase stability suggests an application of lipases from P. citrinum in detergents and other products that require a high stability at room temperature.

Seleçäo de fungos produtores de sacarose fosforilase e sua produçäo a partir do inhame / Screening, thermal properties and production in yam extract of fungal sucrose phosphorylase

Dentre 16 cepas de fungos testados, foram selecionadas 4 cepas como melhores produtoras da atividade sacarose fosforitase.Scytalidium sp e Colletotrichum gloesporioides apresentaram atividade sacarose fosforitase predominantemente intracelular, enquanto que em Sclerotinia sclerotiorum e Monilia sitophila, a atividade foi predominante extracellular.Altos valores de temperatura ótimas 50ºC e 40ºC foram encontrados respectivamente para a enzima de M.sitophila e para as outras 3 cepas selecionadas.Como sacarose fosforilase de M.sitophila foi a mais termoestável, retendo 90-95 por cento de sua atividade fosforolítica inicial após pré-tratamento na ausência de substrato, a 50ºC-70ºC durante 30 minutos, ela foi selecionada para estudos posteriores.A maior produçäo da enzima (340 UI/L de meio cultivado ou 0, 336 UI/mg de proteínas) foi obtida no início da fase estacionária de crescimento da M.sitophila cultivada em extrato de inhame com 0, 15 por cento de sulfato de amônio, à temperatura ambiente(28ºC-30ºC) e agitaçäo continua.Foram afetuados estudos preliminares de imobilizaçäo do extrato bruto da sacarose fosforilase, por adsorçäo em DEAE-celulose e ligaçäo covalente em quitosana.o melhor resultado foi obtido com o derivado imobilizado em quitosana o qual reteve 12 por cento de proteínas e 216 por cento da atividade específica inicial

Giant fibrous polyp of a calyx.

A case of a giant fibrous polyp of the pyelocaliceal system producing hydronephrosis is described. The presentation of the findings in this case as well as brief review of the literature are included.