Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados BJM (2) Ciênc. Tecnol. Aliment. (1) Autor Afzal,Aftab (1) Ahmed,Rafiq (1) Asad,Saeed Ahmad (1) Assis,Sandra Aparecida (1) Barretto,Ingara Keisle São Paulo (1) Gajera,H. P. (1) Hameed,Abdul (1) Hassan,Fayyaz ul (1) Khan,Sabaz Ali (1) Sena,Amanda Reges de (1) Shahzad,Muhammad (1) Tabassum,Ayesha (1) Vakharia,D. N (1) Valasques Júnior,Gildomar Lima (1) Mais... Palavra-chave Lytic enzymes (3) Antagonistic interaction (1) Aspergillus niger (1) Doehlert matrix design (1) Multivariate optimization (1) Mycoparasitic activity (1) Rhizoctonia solani (1) Trichoderma (1) Trichoderma isolates (1) Mais... Tipo do documento Info:eu-repo/semantics/article (3) Ano 2015 (1) 2012 (2) País Brazil (3) Idioma Inglês (3)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 3 Primeira ... 1 ... Última Production of lytic enzymes by Trichoderma isolates during in vitro antagonism with Aspergillus niger, the causal agent of collar rot of peanut BJM Gajera,H. P.; Vakharia,D. N. Twelve isolates of Trichoderma (six of T. harzianum, five of T. viride, one of T. virens), which reduced variably the incidence of collar rot disease caused in peanut by Aspergillus niger Van Tieghem, were evaluated for their potential to produce lytic enzymes during in vitro antagonism. T. viride 60 inhibited highest (86.2%) growth of test fungus followed by T. harzianum 2J (80.4%) at 6 days after inoculation (DAI) on PDA media. The specific activities of chitinase, β-1,3-glucanase and protease were 11, 3.46 and 9 folds higher in T6 antagonist (T. viride 60 and A. niger interactions) followed by 8.72, 2.85 and 9 folds in T8 antagonist (T. harzianum 2J and A. niger interactions), respectively, compared to the activity produced by control petri plate T13... Tipo: Info:eu-repo/semantics/article Palavras-chave: Trichoderma isolates; Aspergillus niger; Lytic enzymes; Antagonistic interaction. Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000100005 Determination of lytic enzyme activities of indigenous Trichoderma isolates from Pakistan BJM Asad,Saeed Ahmad; Tabassum,Ayesha; Hameed,Abdul; Hassan,Fayyaz ul; Afzal,Aftab; Khan,Sabaz Ali; Ahmed,Rafiq; Shahzad,Muhammad. Abstract This study investigated lytic enzyme activities in three indigenous Trichoderma strains namely, Trichoderma asperellum, Trichoderma harzianum and Trichoderma sp. Native Trichoderma strains and a virulent strain of Rhizoctonia solani isolated from infected bean plants were also included in the study. Enzyme activities were determined by measuring sugar reduction by dinitrosalicylic acid (DNS) method using suitable substrates. The antagonists were cultured in minimal salt medium with the following modifications: medium A (1 g of glucose), medium B (0.5 g of glucose + 0.5 g of deactivated R. solani mycelia), medium C (1.0 g of deactivated respective antagonist mycelium) and medium D (1 g of deactivated R. solani mycelia). T asperellum showed presence... Tipo: Info:eu-repo/semantics/article Palavras-chave: Lytic enzymes; Mycoparasitic activity; Rhizoctonia solani; Trichoderma. Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822015000401053 Application of Doehlert experimental design in the optimization of experimental variables for the Pseudozyma sp. (CCMB 306) and Pseudozyma sp. (CCMB 300) cell lysis Ciênc. Tecnol. Aliment. Sena,Amanda Reges de; Valasques Júnior,Gildomar Lima; Barretto,Ingara Keisle São Paulo; Assis,Sandra Aparecida. This study aimed to verify the influence of pH and temperature on the lysis of yeast using experimental design. In this study, the enzymatic extract containing β-1,3-glucanase and chitinase, obtained from the micro-organism Moniliophthora perniciosa, was used. The experiment showed that the best conditions for lysis of Pseudozyma sp. (CCMB 306) and Pseudozyma sp. (CCMB 300) by lytic enzyme were pH 4.9 at 37 ºC and pH 3.9 at 26.7 ºC, respectively. The lytic enzyme may be used for obtaining various biotechnology products from yeast. Tipo: Info:eu-repo/semantics/article Palavras-chave: Lytic enzymes; Multivariate optimization; Doehlert matrix design. Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612012000400019 Registros recuperados: 3 Primeira ... 1 ... Última

Empresa Brasileira de Pesquisa Agropecuária - Embrapa Todos os direitos reservados, conforme Lei n° 9.610 Política de Privacidade Área restrita		Embrapa Parque Estação Biológica - PqEB s/n° Brasília, DF - Brasil - CEP 70770-901 Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco