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Production of thermostable invertases by Aspergillus caespitosus under submerged or solid state fermentation using agroindustrial residues as carbon source; Produção de invertases termoestáveis por Aspergillus caespitosus em fermentação submersa e em estado sólido usando resíduos agroindustriais como fonte de carbono

ALEGRE, Ana Cláudia Paiva; POLIZELI, Maria de Lourdes Teixeira de Moraes; TERENZI, Héctor Francisco; JORGE, João Atílio; GUIMARÃES, Luis Henrique Souza
Fonte: Sociedade Brasileira de Microbiologia Publicador: Sociedade Brasileira de Microbiologia
Tipo: Artigo de Revista Científica
Português
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The filamentous fungus Aspergillus caespitosus was a good producer of intracellular and extracellular invertases under submerged (SbmF) or solid-state fermentation (SSF), using agroindustrial residues, such as wheat bran, as carbon source. The production of extracellular enzyme under SSF at 30ºC, for 72h, was enhanced using SR salt solution (1:1, w/v) to humidify the substrate. The extracellular activity under SSF using wheat bran was around 5.5-fold higher than that obtained in SbmF (Khanna medium) with the same carbon source. However, the production of enzyme with wheat bran plus oat meal was 2.2-fold higher than wheat bran isolated. The enzymatic production was affected by supplementation with nitrogen and phosphate sources. The addition of glucose in SbmF and SSF promoted the decreasing of extracellular activity, but the intracellular form obtained in SbmF was enhanced 3-5-fold. The invertase produced in SSF exhibited optimum temperature at 50ºC while the extraand intracellular enzymes produced in SbmF exhibited maximal activities at 60ºC. All enzymatic forms exhibited maximal activities at pH 4.0-6.0 and were stable up to 1 hour at 50ºC.; O fungo filamentoso Aspergillus caespitosus foi um bom produtor de invertases intracelular e extracelular em fermentação submersa (FSbm) ou em estado sólido (FES)...

Thermostable invertases from Paecylomyces variotii produced under submerged and solid-state fermentation using agroindustrial residues

Giraldo, Marielle Aleixo; Silva, Tony Marcio da; Salvato, Fernanda; Terenzi , Hector Francisco; Jorge, Joao Atilio; Souza Guimaraes, Luis Henrique
Fonte: SPRINGER; NEW YORK Publicador: SPRINGER; NEW YORK
Tipo: Artigo de Revista Científica
Português
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27.72081%
The filamentous fungus Paecylomices variotii was able to produce high levels of cell extract and extracellular invertases when grown under submerged fermentation (SbmF) and solid-state fermentation, using agroindustrial products or residues as substrates, mainly soy bran and wheat bran, at 40A degrees C for 72 h and 96 h, respectively. Addition of glucose or fructose (a parts per thousand yen1%; w/v) in SbmF inhibited enzyme production, while the addition of 1% (w/v) peptone as organic nitrogen source enhanced the production by 3.7-fold. However, 1% (w/v) (NH4)(2)HPO4 inhibited enzyme production around 80%. The extracellular form was purified until electrophoretic homogeneity (10.5-fold with 33% recovery) by DEAE-Fractogel and Sephacryl S-200 chromatography. The enzyme is a monomer with molecular mass of 102 kDa estimated by SDS-PAGE with carbohydrate content of 53.6%. Optima of temperature and pH for both, extracellular and cell extract invertases, were 60A degrees C and 4.0-4.5, respectively. Both invertases were stable for 1 h at 60A degrees C with half-lives of 10 min at 70A degrees C. Mg2+, Ba2+ and Mn2+ activated both extracellular and cell extract invertases from P. variotii. The kinetic parameters K-m and V-max for the purified extracellular enzyme corresponded to 2.5 mM and 481 U/mg prot(-1)...

Reguladores vegetais e atividade de invertases em cana-de-açúcar em meio de safra

Leite, Glauber Henrique Pereira; Crusciol, Carlos Alexandre Costa; Lima, Giuseppina Pace Pereira; Silva, Marcelo de Almeida
Fonte: Universidade Federal de Santa Maria (UFSM) Publicador: Universidade Federal de Santa Maria (UFSM)
Tipo: Artigo de Revista Científica Formato: 718-725
Português
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP); Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq); O objetivo neste trabalho foi a avaliação da atividade das invertases ácida e neutra e a função que essas exercem no controle do acúmulo de sacarose em cana-de-açúcar, variedade SP80-3280, decorrente da aplicação de reguladores vegetais no meio de safra, em Igaraçu do Tietê (SP). O experimento foi conduzido em cana soca, em safras consecutivas (2004 e 2005). O delineamento experimental utilizado foi em blocos casualizados, com cinco repetições. Os tratamentos foram constituídos da aplicação de quatro reguladores vegetais da classe dos retardadores do crescimento (Etefon, Etil-trinexapac, KNO3 e KNO3 + Boro) e uma testemunha (maturação natural), comercialmente encontrados como Ethrel, Moddus, Krista Kana e Krista Kana Plus, respectivamente, adotando-se a dosagem do produto comercial: 2L ha-1, 0,8L ha-1, 3kg ha-1 e 3kg ha-1, respectivamente, sem a adição de adjuvantes. Os reguladores vegetais promovem alterações de intensidades distintas e significativas nos níveis enzimáticos das invertases ácida e neutra. A eficiência agronômica dos maturadores foi afetada de forma significativa pelo clima e pela época de aplicação. Os tratamentos com maturadores...

Atividade das enzimas invertases e acúmulo de sacarose em cana-de-açúcar sob efeito do nitrato de potássio, etefon e etil-trinexapac

Leite, Glauber Henrique Pereira; Crusciol, Carlos Alexandre Costa; Silva, Marcelo de Almeida; Lima, Giuseppina Pace Pereira
Fonte: Editora da Universidade Federal de Lavras (UFLA) Publicador: Editora da Universidade Federal de Lavras (UFLA)
Tipo: Artigo de Revista Científica Formato: 649-656
Português
Relevância na Pesquisa
27.72081%
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP); Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq); Conduziu-se este trabalho, com o objetivo de avaliar a atividade das enzimas invertases ácida e neutra e sua influência no processo de regulação do acúmulo de sacarose nos colmos da cana-de-açúcar, cultivar RB855453, sob efeito do nitrato de potássio comparado aos maturadores, da classe dos retardantes do crescimento, etefon e etil-trinexapac, buscando contribuir para o entendimento da ação desse composto químico. Os tratamentos constituíram-se da aplicação de quatro maturadores da classe dos retardantes do crescimento, cujos ingredientes ativos são etefon, etil-trinexapac, nitrato de potássio e nitrato de potássio + boro, e a maturação natural como testemunha, em delineamento experimental em blocos casualizados com cinco repetições. Os níveis enzimáticos das invertases ácida e neutra foram afetados de forma e intensidade distintas em função do princípio ativo utilizado como maturador e das condições climáticas; contudo, de forma geral, os níveis da invertase ácida manifestaram-se superiores aos da invertase neutra sem comprometer o acúmulo de sacarose nos colmos da cana-de-açúcar cultivar RB855453. O nitrato de potássio apresentou efeito maturador na cultura da cana-de-açúcar possibilitando o acúmulo de sacarose nos colmos...

Thermostable invertases from Paecylomyces variotii produced under submerged and solid-state fermentation using agroindustrial residues

Giraldo, Marielle Aleixo; da Silva, Tony Marcio; Salvato, Fernanda; Terenzi, Hector Francisco; Jorge, Joao Atilio; Souza Guimaraes, Luis Henrique
Fonte: Springer Publicador: Springer
Tipo: Artigo de Revista Científica Formato: 463-472
Português
Relevância na Pesquisa
27.72081%
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP); The filamentous fungus Paecylomices variotii was able to produce high levels of cell extract and extracellular invertases when grown under submerged fermentation (SbmF) and solid-state fermentation, using agroindustrial products or residues as substrates, mainly soy bran and wheat bran, at 40A degrees C for 72 h and 96 h, respectively. Addition of glucose or fructose (a parts per thousand yen1%; w/v) in SbmF inhibited enzyme production, while the addition of 1% (w/v) peptone as organic nitrogen source enhanced the production by 3.7-fold. However, 1% (w/v) (NH4)(2)HPO4 inhibited enzyme production around 80%. The extracellular form was purified until electrophoretic homogeneity (10.5-fold with 33% recovery) by DEAE-Fractogel and Sephacryl S-200 chromatography. The enzyme is a monomer with molecular mass of 102 kDa estimated by SDS-PAGE with carbohydrate content of 53.6%. Optima of temperature and pH for both, extracellular and cell extract invertases, were 60A degrees C and 4.0-4.5, respectively. Both invertases were stable for 1 h at 60A degrees C with half-lives of 10 min at 70A degrees C. Mg2+, Ba2+ and Mn2+ activated both extracellular and cell extract invertases from P. variotii. The kinetic parameters K-m and V-max for the purified extracellular enzyme corresponded to 2.5 mM and 481 U/mg prot(-1)...

Estudos preliminares sobre as invertases de cafeeiros atacados por Hemileia vastatrix

Carvalho,Paulo de Campos Torres de
Fonte: Universidade de São Paulo; Escola Superior de Agricultura Publicador: Universidade de São Paulo; Escola Superior de Agricultura
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/01/1972 Português
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No presente trabalho, que o autor considera exploratório, foram estudadas as invertases presentes em folhas de cafeeiros das variedades Geisha (SH1 SH5) e Kent (SH2 SH5), inoculados com as raças III (n1 n5) e XXIV (n2 n4) de Hemileia vastatrix. Devido ao genótipo do material utilizado as reações são opostas, ou seja, o cafeeiro Kent é resistente à raça III e suscetível à raça XXIV e o Geisha o contrário. Em cada par de folhas, uma foi inoculada e outra mantida como controle e a determinação das invertases foi feita aos 6 e 16 dias após a inoculação. Os resultados preliminares obtidos mostraram que, independente da variedade de cafeeiro ou da raça de Hemileia vastatrix, nas combinações suscetíveis não houve alteração das invertases presentes, iguais às de plantas sadias, com o máximo de atividade em pH 4,5. Já nas combinações resistentes no 6.º dia após a inoculação houve o aparecimento de uma "invertase ácida pH 4,0", ausente tanto nas plantas sadias como nas combinações suscetíveis das mesmas variedades. O aparecimento da "invertase ácida pH 4,0" está relacionado com a diminuição do teor de sacarose nas folhas. Quanto ao significado desta "invertase ácida pH 4,0" na patogenese da ferrugem do cafeeiro...

Metabolismo de carboidratos durante o amadurecimento do mamão (Carica papaya L. Cv. Solo): influência da radiação gama

GOMEZ,M. L. P. A.; LAJOLO,F. M.; CORDENUNSI,B. R.
Fonte: Sociedade Brasileira de Ciência e Tecnologia de Alimentos Publicador: Sociedade Brasileira de Ciência e Tecnologia de Alimentos
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/05/1999 Português
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A irradiação de alimentos é um tratamento pós-colheita bastante promissor, capaz de atuar tanto na desinfestação como no aumento da vida útil de frutos. O mamão é um fruto com curta vida pós-colheita, levando de 6 a 12 dias para atingir a senescência. Além disto, a infestação por larvas de mosca diminui sensivelmente o seu potencial de exportação. O objetivo deste trabalho foi verificar a ação de uma dose de 0,5 kGy de irradiação gama, normalmente utilizada para desinfestação e aumento de vida útil dos frutos, sobre o comportamento dos carboidratos solúveis durante o amadurecimento do mamão (Carica papaya L. cv. Solo), e sobre as enzimas relacionadas ao metabolismo da sacarose: sacarose sintase (SS), sacarose-fosfato sintase (SPS) e invertases ácida e neutra. Os resultados demonstraram que a irradiação não exerce efeito sobre o teor de glicose e frutose, ou sobre a respiração e atividade da SS. Entretanto, a composição dos açúcares solúveis totais e da sacarose, e a atividade da SPS e das invertases foram afetados.

Reguladores vegetais e atividade de invertases em cana-de-açúcar em meio de safra

Leite,Glauber Henrique Pereira; Crusciol,Carlos Alexandre Costa; Lima,Giuseppina Pace Pereira; Silva,Marcelo de Almeida
Fonte: Universidade Federal de Santa Maria Publicador: Universidade Federal de Santa Maria
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/06/2009 Português
Relevância na Pesquisa
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O objetivo neste trabalho foi a avaliação da atividade das invertases ácida e neutra e a função que essas exercem no controle do acúmulo de sacarose em cana-de-açúcar, variedade SP80-3280, decorrente da aplicação de reguladores vegetais no meio de safra, em Igaraçu do Tietê (SP). O experimento foi conduzido em cana soca, em safras consecutivas (2004 e 2005). O delineamento experimental utilizado foi em blocos casualizados, com cinco repetições. Os tratamentos foram constituídos da aplicação de quatro reguladores vegetais da classe dos retardadores do crescimento (Etefon, Etil-trinexapac, KNO3 e KNO3 + Boro) e uma testemunha (maturação natural), comercialmente encontrados como Ethrel, Moddus, Krista Kana e Krista Kana Plus, respectivamente, adotando-se a dosagem do produto comercial: 2L ha-1, 0,8L ha-1, 3kg ha-1 e 3kg ha-1, respectivamente, sem a adição de adjuvantes. Os reguladores vegetais promovem alterações de intensidades distintas e significativas nos níveis enzimáticos das invertases ácida e neutra. A eficiência agronômica dos maturadores foi afetada de forma significativa pelo clima e pela época de aplicação. Os tratamentos com maturadores, principalmente em 2004, cujas condições climáticas foram desfavoráveis à maturação natural...

Atividade das enzimas invertases e acúmulo de sacarose em cana-de-açúcar sob efeito do nitrato de potássio, etefon e etil-trinexapac

Leite,Glauber Henrique Pereira; Crusciol,Carlos Alexandre Costa; Silva,Marcelo de Almeida; Lima,Giuseppina Pace Pereira
Fonte: Editora da Universidade Federal de Lavras Publicador: Editora da Universidade Federal de Lavras
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/08/2011 Português
Relevância na Pesquisa
27.40986%
Conduziu-se este trabalho, com o objetivo de avaliar a atividade das enzimas invertases ácida e neutra e sua influência no processo de regulação do acúmulo de sacarose nos colmos da cana-de-açúcar, cultivar RB855453, sob efeito do nitrato de potássio comparado aos maturadores, da classe dos retardantes do crescimento, etefon e etil-trinexapac, buscando contribuir para o entendimento da ação desse composto químico. Os tratamentos constituíram-se da aplicação de quatro maturadores da classe dos retardantes do crescimento, cujos ingredientes ativos são etefon, etil-trinexapac, nitrato de potássio e nitrato de potássio + boro, e a maturação natural como testemunha, em delineamento experimental em blocos casualizados com cinco repetições. Os níveis enzimáticos das invertases ácida e neutra foram afetados de forma e intensidade distintas em função do princípio ativo utilizado como maturador e das condições climáticas; contudo, de forma geral, os níveis da invertase ácida manifestaram-se superiores aos da invertase neutra sem comprometer o acúmulo de sacarose nos colmos da cana-de-açúcar cultivar RB855453. O nitrato de potássio apresentou efeito maturador na cultura da cana-de-açúcar possibilitando o acúmulo de sacarose nos colmos...

Rapid Repression of Maize Invertases by Low Oxygen. Invertase/Sucrose Synthase Balance, Sugar Signaling Potential, and Seedling Survival1

Zeng, Ying; Wu, Yong; Avigne, Wayne T.; Koch, Karen E.
Fonte: American Society of Plant Physiologists Publicador: American Society of Plant Physiologists
Tipo: Artigo de Revista Científica
Publicado em /10/1999 Português
Relevância na Pesquisa
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We show here that invertase gene expression and the invertase-sucrose (Suc) synthase ratio decrease abruptly in response to low oxygen in maize root tips. In addition to aiding in the conservation of carbon and possibly ATP, this response has the potential to directly affect sugar signaling relative to carbon flux. Experiments were motivated by the potential for a reduced invertase/Suc synthase balance to alter the impact of respiratory and/or membrane carbon flux on sugar signaling. Maize (Zea mays L.) seedlings with 5-cm primary roots were exposed to anoxic (0% [v/v] O2), hypoxic (3% [v/v] O2), and aerobic conditions. Rapid repression of the Ivr1 and Ivr2 maize invertases by low oxygen was evident in root tips within 3 h at both the transcript and activity levels. The speed and extent of this response increased with the degree of oxygen deprivation and differed with genotypes. This decrease in expression also contrasted markedly to that of other genes for respiratory Suc metabolism, such as Suc synthases, which typically increased or remained constant. Although previous work showed that the contrasting effects of sugars on Suc synthase genes were reflected in their regulation by hypoxia and anoxia, the same was not observed for the differentially sugar-responsive invertases. Theoretically advantageous reductions in the invertase/Suc synthase balance thus resulted. However...

Purification and characterization of three soluble invertases from barley (Hordeum vulgare L.) leaves.

Obenland, D M; Simmen, U; Boller, T; Wiemken, A
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /04/1993 Português
Relevância na Pesquisa
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Three soluble isoforms of invertase (beta-fructofuranosidase; EC 3.2.1.26) were purified from 7-d-old primary leaves of barley (Hordeum vulgare L.). Invertase I, a monomeric protein of 64 kD, was purified to apparent homogeneity as shown by sodium dodecylsulfate-polyacrylamide gel electrophoresis. Invertases IIA and IIB, multimeric proteins with molecular masses of the 116 and 155 kD, were purified 780- and 1370-fold, respectively, but were not yet homogeneous. Extracts of epidermal strips of leaves contained only invertase IIB. The specific activity of invertase was more than 100-fold higher in the epidermis than in the mesophyll. All three isoforms were acidic invertases, with pH optima of around 5.0 and little activity in the alkaline range. Invertase I had a Km for sucrose of 8.1 mM, and invertases IIA and IIB had much lower values of 1.0 and 1.7 mM, respectively. Invertase I was more than 2-fold more resistant than the other two invertases to the inhibitors HgCl2 and pyridoxal. All three constitutive invertases were found to act also as sucrose-sucrose fructosyltransferases when supplied with high concentrations of sucrose, forming 1-kestose as principal product. However, the fructosyltransferase activity of all three enzymes was inhibited by pyridoxal in the same way as their invertase activity. This characteristic clearly differentiates them from the inducible sucrose-sucrose fructosyltransferase of barley leaves...

Comparative Study of Invertases of Streptococcus mutans

Tanzer, J. M.; Brown, A. T.; McInerney, M. F.; Woodiel, F. N.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /04/1977 Português
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Sucrase activity was studied in 13 strains of Streptococcus mutans representing the five Bratthall serotypes. Sucrose-adapted cells have sucrase activity in the 37,000 × g-soluble fraction of all strains. The enzyme was identified as invertase (β-d-fructofuranoside fructohydrolase; EC 3.2.1.26) because it hydrolyzed the β-fructofuranoside trisaccharide raffinose, giving fructose and melibiose as its products, and because it hydrolyzed the β-fructofuranoside dissacharide sucrose, giving equimolar glucose and fructose as its products. Invertases of c and e strains exhibit two activity peaks by molecular exclusion chromatography with molecular weights of 45,000 to 50,000 and about 180,000; those of serotypes a, b, and d strains exhibit only a single component of 45,000 to 50,000 molecular weight. The electrophoretic mobility of invertases is different between the serotypes and the same within them. Inorganic orthophosphate (Pi) has a weak positive effect on the Vmax of invertases of serotypes c and e cells but a strong positive effect on the invertases of serotype b cells; Pi has a strong positive effect on the apparent Km of the invertases of serotype d cells, but has no effect on the Vmax; Pi has a strong positive effect on both the apparent Km and Vmax of the invertases of serotype a cells. Thus...

Invertases in Oat Seedlings: SEPARATION, PROPERTIES, AND CHANGES IN ACTIVITIES IN SEEDLING SEGMENTS

Pressey, Russell; Avants, Jimmy K.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /01/1980 Português
Relevância na Pesquisa
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The soluble invertase activity in etiolated Avena seedlings was highest at the apex of the coleoptile and much lower in the primary leaf, mesocotyl, and root. The activity in all parts of the seedling consisted of two invertases (I and II) which were separated by chromatography on diethylaminoethylcellulose. Both enzymes appeared to be acid invertases, but they differed in molecular size, pH optimum, and the kinetic parameters Km and Vmax of their action on sucrose, raffinose, and stachyose. Invertase II had low stability at pH 3.5 and below, and exhibited high sensitivity to Hg2+, with complete inhibition by 2 micromolar HgCl2. Segments of coleoptiles incubated in water lost about two-thirds of the total invertase activity after 16 hours. The loss of activity was due primarily to a decrease in the level of invertase II. The loss of invertase was decreased by indoleacetic acid, 2,4-dichlorophenoxyacetic acid, and α-naphthaleneacetic acid but not by β-naphthaleneacetic acid and p-chlorophenoxyisobutyric acid. Conditions that inhibited auxin-induced growth of the segments (20 millimolar CaCl2 and 200 millimolar mannitol) also blocked the auxin effect on invertase loss.

Host-Pathogen Interactions: XIII. Extracellular Invertases Secreted by Three Races of a Plant Pathogen Are Glycoproteins Which Possess Different Carbohydrate Structures 1

Ziegler, Ernst; Albersheim, Peter
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /06/1977 Português
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The invertase present in the culture fluid of races 1, 2, and 3 of Phytophthora megasperma Drechs. var. sojae A. A. Hildebrand (Pms) were purified until they gave but a single band, whether stained for protein or carbohydrate, after isoelectric focusing in flat bed gels. The sugar compositions of multiple preparations of the purified invertases from each race of this fungal pathogen were determined by quantitative gas chromatography of their alditol acetates. The invertases are composed of about 25% carbohydrate. Mannose and glucosamine make up more than 97% of the carbohydrate portions of the invertases of all three Pms races analyzed, but the ratio of mannose to glucosamine is clearly not the same in each race. The glycosyl linkage compositions of the glucosamine-containing mannans of multiple preparations of the Pms invertases were determined by GC-MS analysis of the partially methylated alditol acetate derivatives. The results of these analyses demonstrate clear quantitative differences between the glycosyl components of the different Pms races. The existence of race-specific carbohydrate structures in the differentially virulent Pms races suggests that these carbohydrates may be involved in determining the specificity of hostpathogen interactions.

Acid and Alkaline Invertases in Suspension Cultures of Sugar Beet Cells

Masuda, Hiroshi; Takahashi, Toshimasa; Sugawara, Shiro
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /01/1988 Português
Relevância na Pesquisa
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Alkaline invertase was induced during the initiation of suspension cultures of single cells from leaf explants of sugar beets in Murashige-Skoog liquid medium which contained benzyladenine. This activity was barely detectable in the leaves themselves. In suspension cultures, the presence of both acid and alkaline invertases was detected; alkaline invertase was only present in the cytoplasm of the cultured cells, whereas acid invertase was present in the cytoplasm and cell walls, and was also detected in the culture medium. The cell wall contained at least three types of acid invertase; two of these activities were solubilized by saline (saline-released) and EDTA (EDTA-released), respectively, and the third remained tightly associated with the cell wall. Saline-released and EDTA-released invertases from the cell wall showed the significant differences in their properties: the saline-released enzyme had the highest affinity for sucrose among the invertases tested, and was easily bound to cell walls, to DNA, and to a cation exchanger, unlike the EDTA-released enzyme. Sucrose is the source of carbon for plant cells in suspension culture and is probably degraded in the cell wall by the saline-released invertase, which had the highest activity and the highest affinity for sucrose. Hexose products of this degradation would be transported to cytoplasm. Soluble invertase...

Acid and Neutral Invertases in the Mesocarp of Developing Muskmelon (Cucumis melo L. cv Prince) Fruit

Ranwala, Anil P.; Iwanami, Shun-Suke; Masuda, Hiroshi
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /07/1991 Português
Relevância na Pesquisa
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Acid and neutral invertases were found in the mesocarp of developing muskmelon (Cucumis melo L. cv Prince) fruit and the activities of these enzymes declined with maturation of the fruit, concomitantly with the accumulation of sucrose. Neutral invertase was only present in the soluble fraction and acid invertase was present in both the soluble and cell-wall fractions. The cell-wall fraction contained three types of acid invertase: a NaCl-released invertase; an EDTA-released invertase, and a tightly bound invertase that still remained on the cell wall after treatment with NaCl and EDTA. The soluble acid and neutral invertases could be separated from one another by chromatography on DEAE-cellulose and they exhibited clear differences in their properties, namely, in their pH optima, substrate specificity, Km values for sucrose, and inhibition by metal ions. The EDTA-released invertase and the soluble acid invertase were similar with regard to their chromatographic behavior on DEAE-cellulose, but the NaCl-released invertase was different because it was adsorbed to a column of CM-cellulose. The soluble acid invertase and two cell-wall bound invertases had very similar characteristics with regard to optimal pH and temperature, Km value for sucrose...

Invertase Inhibitor from Potatoes: Purification, Characterization, and Reactivity with Plant Invertases

Pressey, Russell
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /12/1967 Português
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Invertase inhibitor was extracted from potato tubers and purified nearly 1000-fold. The purification procedure involved precipitation at pH 4.0, fractionation with ammonium sulfate, adsorption on alumina Cγ gel, and gel filtration on Sephadex G-100 and DEAE-Sephadex A-50. The product obtained was homogeneous to electrophoresis on polyacrylamide gel. Exclusion chromatography on Sephadex G-100 indicated a molecular weight of about 17,000. The inhibitor did not inhibit yeast, Neurospora, and several plant invertases. It completely inhibited potato tuber invertase and a number of other plant invertases. Some plant invertases were partially inhibited.

Unraveling the Difference between Invertases and Fructan Exohydrolases: A Single Amino Acid (Asp-239) Substitution Transforms Arabidopsis Cell Wall Invertase1 into a Fructan 1-Exohydrolase1[C]

Le Roy, Katrien; Lammens, Willem; Verhaest, Maureen; De Coninck, Barbara; Rabijns, Anja; Van Laere, André; Van den Ende, Wim
Fonte: American Society of Plant Biologists Publicador: American Society of Plant Biologists
Tipo: Artigo de Revista Científica
Publicado em /11/2007 Português
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Plant cell wall invertases and fructan exohydrolases (FEHs) are very closely related enzymes at the molecular and structural level (family 32 of glycoside hydrolases), but they are functionally different and are believed to fulfill distinct roles in plants. Invertases preferentially hydrolyze the glucose (Glc)-fructose (Fru) linkage in sucrose (Suc), whereas plant FEHs have no invertase activity and only split terminal Fru-Fru linkages in fructans. Recently, the three-dimensional structures of Arabidopsis (Arabidopsis thaliana) cell wall Invertase1 (AtcwINV1) and chicory (Cichorium intybus) 1-FEH IIa were resolved. Until now, it remained unknown which amino acid residues determine whether Suc or fructan is used as a donor substrate in the hydrolysis reaction of the glycosidic bond. In this article, we present site-directed mutagenesis-based data on AtcwINV1 showing that the aspartate (Asp)-239 residue fulfills an important role in both binding and hydrolysis of Suc. Moreover, it was found that the presence of a hydrophobic zone at the rim of the active site is important for optimal and stable binding of Suc. Surprisingly, a D239A mutant acted as a 1-FEH, preferentially degrading 1-kestose, indicating that plant FEHs lacking invertase activity could have evolved from a cell wall invertase-type ancestor by a few mutational changes. In general...

Molecular and Functional Characterization of Novel Fructosyltransferases and Invertases from Agave tequilana

Cortés-Romero, Celso; Martínez-Hernández, Aída; Mellado-Mojica, Erika; López, Mercedes G.; Simpson, June
Fonte: Public Library of Science Publicador: Public Library of Science
Tipo: Artigo de Revista Científica
Publicado em 30/04/2012 Português
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Fructans are the main storage polysaccharides found in Agave species. The synthesis of these complex carbohydrates relies on the activities of specific fructosyltransferase enzymes closely related to the hydrolytic invertases. Analysis of Agave tequilana transcriptome data led to the identification of ESTs encoding putative fructosyltransferases and invertases. Based on sequence alignments and structure/function relationships, two different genes were predicted to encode 1-SST and 6G-FFT type fructosyltransferases, in addition, 4 genes encoding putative cell wall invertases and 4 genes encoding putative vacuolar invertases were also identified. Probable functions for each gene, were assigned based on conserved amino acid sequences and confirmed for 2 fructosyltransferases and one invertase by analyzing the enzymatic activity of recombinant Agave protein s expressed and purified from Pichia pastoris. The genome organization of the fructosyltransferase/invertase genes, for which the corresponding cDNA contained the complete open reading frame, was found to be well conserved since all genes were shown to carry a 9 bp mini-exon and all showed a similar structure of 8 exons/7 introns with the exception of a cell wall invertase gene which has 7 exons and 6 introns. Fructosyltransferase genes were strongly expressed in the storage organs of the plants...

Estudos preliminares sobre as invertases de cafeeiros atacados por Hemileia vastatrix; Preliminary studies on the invertases of coffee plants infected by Hemileia vastatrix

Carvalho, Paulo de Campos Torres de
Fonte: Universidade de São Paulo. Escola Superior de Agricultura Luiz de Queiroz Publicador: Universidade de São Paulo. Escola Superior de Agricultura Luiz de Queiroz
Tipo: info:eu-repo/semantics/article; info:eu-repo/semantics/publishedVersion; ; ; ; Formato: application/pdf
Publicado em 01/01/1972 Português
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No presente trabalho, que o autor considera exploratório, foram estudadas as invertases presentes em folhas de cafeeiros das variedades Geisha (SH1 SH5) e Kent (SH2 SH5), inoculados com as raças III (n1 n5) e XXIV (n2 n4) de Hemileia vastatrix. Devido ao genótipo do material utilizado as reações são opostas, ou seja, o cafeeiro Kent é resistente à raça III e suscetível à raça XXIV e o Geisha o contrário. Em cada par de folhas, uma foi inoculada e outra mantida como controle e a determinação das invertases foi feita aos 6 e 16 dias após a inoculação. Os resultados preliminares obtidos mostraram que, independente da variedade de cafeeiro ou da raça de Hemileia vastatrix, nas combinações suscetíveis não houve alteração das invertases presentes, iguais às de plantas sadias, com o máximo de atividade em pH 4,5. Já nas combinações resistentes no 6.º dia após a inoculação houve o aparecimento de uma "invertase ácida pH 4,0", ausente tanto nas plantas sadias como nas combinações suscetíveis das mesmas variedades. O aparecimento da "invertase ácida pH 4,0" está relacionado com a diminuição do teor de sacarose nas folhas. Quanto ao significado desta "invertase ácida pH 4,0" na patogenese da ferrugem do cafeeiro...