Sucrose hydrolysis by gelatin-immobilized inulinase from Kluyveromyces marxianus var. bulgaricus

Paula, Fabrício Coutinho de; Cazetta, Márcia Luciana; Monti, Rubens; Contiero, Jonas

doi:10.1016/j.foodchem.2008.04.039

Cited by 35 publications

(31 citation statements)

References 28 publications

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“…Among the chemicals used to crosslink gelatin, glutaraldehyde has been used extensively because it has the advantage of being a fast-acting hardener for colageneous materials (Martucci et al, 2006). For the matrix in which glutaraldehyde was used, after cooling, 10 mL of a 2.5% (v/v) glutaraldehyde solution (Paula et al, 2008) were added on one surface and the samples were stored for 30 min. They were then washed with distilled water.…”

Section: Preparation Of Matrices and Lipase Immobilizationmentioning

confidence: 99%

Influence of bloom number and plastifiers on gelatin matrices produced for enzyme immobilization

Kempka

Souza

et al. 2014

Braz. J. Chem. Eng.

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-In this study the immobilization of lipase in matrices produced with gelatin with different Bloom values and with the addition of plastifiers was investigated to evaluate the influence of the Bloom value, as well as the capacity of the plastifiers to maintain the enzyme immobilized and the immobilization yield. The results indicated the need for crosslinking of the matrices with glutaraldehyde due to the high solubility in water, explained by the amino acid profile, which confirms the solubility of gelatin. Mannitol showed greater efficiency in the lipase immobilization, since it led to more porous structures and more uniform pores. These structures were also influenced by the gelatin concentration; greater concentrations associated with intermediate concentrations of plastifier led to matrices with a greater immobilization yield (87.92%). The X-ray diffraction analysis revealed that the structure of the immobilization matrices was partially crystalline.

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Section: Preparation Of Matrices and Lipase Immobilizationmentioning

confidence: 99%

Influence of bloom number and plastifiers on gelatin matrices produced for enzyme immobilization

Kempka

Souza

et al. 2014

Braz. J. Chem. Eng.

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“…The effect of pH (2.5-8.0) for an inulinase of K. marxianus var. bulgaricus immobilized in gelatin was evaluated by Paula et al [20]. High enzyme activities were obtained in pH value of 3.5.…”

Section: Stability Of the Immobilization Processmentioning

confidence: 99%

Immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571 using modified sodium alginate beads

Richetti

Munaretto

Lerin

et al. 2011

Bioprocess Biosyst Eng

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An experimental design was carried out to evaluate the effect of the concentrations of sodium alginate, glutaraldehyde and activated coal on the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571. The experimental condition of 20 g/L of sodium alginate, 50 mL/L of glutaraldehyde and 30 g/L of activated coal led to the highest specific activity (2,063.5 U/mg of protein), corresponding to an enhancement of about 26 times compared to the activity of the free enzyme (79.1 U/mg of protein). The effect of pH and temperature on the immobilized enzyme activity was also evaluated, showing optimal activities at pH of 5.5 and 55 °C. The study of storage of immobilized inulinase in different temperatures showed that the extract kept its initial activity after 43 days of storage at 40 and 50 °C and after 138 days of storage either at 4 or 25 °C.

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“…bulgaricus ATCC 16045 en presencia de inulina y sacarosa siendo 86.9 mg/ml y 53.7 U/mg de proteína y 4.58 mg/ml y 441.0 U/mg de proteína a 55 ºC y pH 4.4 óptimos, respectivamente, demostrando que la enzima producida es una exo-inulinasa con más alta afinidad y reactividad por la sacarosa que por la inulina. De Paula et al (2008) también determinaron los valores de los parámetros cinéticos de un caldo crudo exento de células conteniendo inulinasa de Kluyveromyces marxianus var. bulgaricus ATCC 16045 siendo de K m igual a 61.83 mM y V max igual a 37.60 U/mg de proteína a 55 ºC y pH 3.5 óptimos.…”

Section: Caracterización Y Propiedades De La Inulinasaunclassified

“…Sus parámetros cinéticos fueron de K m igual a 149.28 mM y V max igual a 31.45 U/mg de proteína a 55 ºC y pH 3.5 óptimos. La inulinasa inmovilizada actuó con una eficiencia de conversión de sacarosa del 58.12 % en un reactor continuo de lecho fijo operando por 33 días (de Paula et al, 2008). Células de Kluyveromyces marxianus con actividad de inulinasa, fueron inmovilizados en alginato de bario tratado con glutaraldehído, manteniéndose una actividad residual del 85 % y una eficiencia del sistema (η) de 0.79 para un diámetro de partícula de 1.43 mm.…”

Section: Inmovilizaciónunclassified

Inulinase production by yeat Kluyveromyces marxianus

Castillo

Chamy

2010

Sci. agropecu

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Recibido 04 agosto 2010; aceptado 22 octubre 2010 ResumenEn este trabajo se han revisado los principales avances alcanzados en los últimos veinte años, en el estudio de la fermentación de cepas de Kluyveromyces marxianus para la producción de la enzima inulinasa a partir de inulina pura y fuentes de inulina y la determinación de las propiedades y características de la enzima. Con el propósito de recopilar y esclarecer el mayor conocimiento de ésta área, la investigación de ésta materia ha sido dividida en tres partes: sustratos fuentes de inulina; producción microbiana de inulinasa y caracterización y propiedades de la inulinasa. Se discute la información existente sobre los microorganismos capaces de producir inulinasa los que han sido publicados con datos de rendimiento y en particular las condiciones de fermentación de cepas de Kluyveromyces marxianus para la producción de inulinasa a partir de varias fuentes vegetales de inulina. Se concluye que si bien es cierto existen cepas de Kluyveromyces marxianus capaces de producir satisfactoriamente inulinasa, la investigación para una fuente vegetal de inulina económicamente interesante todavía está en curso. Palabras clave: Kluyveromyces marxianus, inulinasa, inulina. AbstractIn this work the principal advances have been checked reached in the last twenty years, in the study of the fermentation of strains of Kluyveromyces marxianus for the production of the enzyme inulinase from inulin pure and sources of inulina and the determination of the properties and characteristics of the enzyme. With the aim of gathering and clarifying the greater knowledge of this one area, the investigation of this matter has been divided into three principal parts; substrate sources of inulin; microbial production of inulinase and characterization and properties of the inulinase. There is discussed the existing information about the microorganisms capable of producing inulinase those who have been brought by information of performance and especially the conditions of fermentation of strains of Kluyveromyces marxianus for the production of inulinase from several vegetable sources of inulin. One concludes that though it is true there exist strains of Kluyveromyces marxianus capable of producing satisfactorily inulinase, the investigation for a vegetable source of inulin economically interesting still is in process.

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Sucrose hydrolysis by gelatin-immobilized inulinase from Kluyveromyces marxianus var. bulgaricus

Cited by 35 publications

References 28 publications

Influence of bloom number and plastifiers on gelatin matrices produced for enzyme immobilization

Influence of bloom number and plastifiers on gelatin matrices produced for enzyme immobilization

Immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571 using modified sodium alginate beads

Inulinase production by yeat Kluyveromyces marxianus

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