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Regulation of xylanase in Aspergillus phoenicis: a physiological and molecular approach
J Ind Microbiol Biotechnol (2008) 35:237–244
Ana Carolina Segato Rizzatti · Fernanda Zanolli Freitas · Maria Célia Bertolini · Simone Carvalho Peixoto-Nogueira · Héctor Francisco Terenzi · João Atílio Jorge · Maria de Lourdes Teixeira de Moraes Polizeli
Microbial xylanolytic enzymes have a promising biotechnological potential, and are extensively applied in industries. In this study, induction of xylanolytic activity was examined in Aspergillus phoenicis. Xylanase activity induced by xylan, xylose or beta-methylxyloside was predominantly extracellular (93–97%). Addition of 1% glucose to media supplemented with xylan or xylose repressed xylanase production. Glucose
Screening of filamentous fungi for production of enzymes of biotechnological interest
Brazilian Journal of Microbiology (2006) 37:474-480
Luis Henrique S. Guimarães; Simone C. Peixoto-Nogueira; Michele Michelin; Ana Carolina S. Rizzatti; Valéria C. Sandrim; FabianaF. Zanoelo; Ana Carla M.M. Aquino; Altino B. Junior; Maria de Lourdes T.M. Polizeli
Many enzymes produced by fungi have relevant biotechnological applications in several industrial areas. The purpose of this study was to collect and isolate filamentous fungi from soil and humus, plants and sugar cane bagasse of different regions of the São Paulo state. Forty isolates were examined for their ability to produce xylanase, glucose-oxidase, alkaline phosphatase, acid phosphatase, phytase, pectinase and amylase. Among these, twenty three isolates exhibited enzymatic potential. The xylanases produced by two of these isolates (Aspergillus caespitosus and A. phoenicis) showed good potential for pulp bleaching. Among seventeen isolates, at least three produced high levels of glucose-oxidase, being Rhizopus stolonifer and A. versicolor the best producer strains. A. caespitosus, Mucor rouxii, and nine others still not identified were the best
Biotecnologia
O assunto BIOTECNOLOGIA está "em alta". Na internet podemos encontrar vários videos e/ou apresentações de slides muito importantes sobre o assunto. O link abaixo mostra uma apresentação de slides muito interessante que mostra de maneira simples, clara e bastante ilustrativa do que se trata a biotecnologia.
Este vídeo é da autoria de terceiros e os nomes dos autores deste trabalho aparecem no final da apresentação.
Glucoamylase isoform (GAII) purified from a thermophilic fungus Scytalidium thermophilum 15.8 with biotechnological potential
AFRICAN JOURNAL OF BIOTECHNOLOGY 5(12):1239-1245 (2006)
Mariana Cereia; Luis Henrique S. Guimarães; Simone C. Peixoto-Nogueira; João A. Jorge; Héctor F. Terenzi; Lewis J. Greene; Maria de Lourdes T.M. Polizeli
Scytalidium thermophilum 15.8 produced two extracellular glucoamylases. Using a DEAE-Cellulose chromatographic column glucoamylases form II (GAII) was separated and purified from glucoamylases form I (GAI) that was previously purified and characterised (Cereia et al., 2000) when the filtrate of the culture medium was applied to a DEAE-Cellulose
Aplicação biotecnológica de enzimas na indústria de rações
As xilanases podem ser aplicadas como aditivo em ração para ruminantes, no intuito de aumentar a digestibilidade de alimentos fibrosos e, consequentemente, o desempenho animal. Essas enzimas atuam degradando os carboidratos ingeridos no alimento e fornecem açúcares menores para as bactérias presentes no rúmen bovino. Na presença desses oligossacarídeos rapidamente assimiláveis, há uma maior e mais rápida proliferação das bactérias no rúmen aumentando a eficiência do processo de digestão.
Characterisation of an acid trehalase produced by the thermotolerant fungus Rhizopus microsporus var. rhizopodiformis: Biochemical properties and immunochemical localisation
FEMS MICROBIOLOGY LETTERS 251 (2005) 169–175
Ana Carla Medeiros Morato de Aquino, Simone Carvalho Peixoto-Nogueira, João Atílio Jorge, Héctor Francisco Terenzi, Maria de Lourdes Teixeira de Moraes Polizeli
An acid trehalase from Rhizopus microsporus var. rhizopodiformis was purified to apparent homogeneity. The molecular weight by SDS–PAGE (60 kDa) or Sephacryl S-200 filtration (105 kDa) suggested a homodimer. The carbohydrate content was 72%. Endoglycosidase H digestion resulted in one sharp band of 51.5 kDa in SDS–PAGE. pH and temperature optima were 4.5 and 45ºC, respectively. The isoelectric point was 6.69 and activation energy was 1.14 kcal mol-1. The enzyme was stable for 1 h at 50ºC and decayed at 60ºC (t50 of 1.3 min.). Apparent KM for trealose was 0.2 mM. Immunolocalisation studies showed the enzyme tightly packed at the surface of the cells.
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