Purification of papain from fresh latex of Carica papaya

Monti, Rubens; Basilio, C.; Trevisan, Henrique C.; Contiero, Jonas

doi:10.1590/s1516-89132000000500009

Cited by 40 publications

(28 citation statements)

References 16 publications

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“…It is used to tenderize meat and meat products, in the manufacture of protein hydrolysate, in brewing industry for clarifying juice and beer, in dairy industry for cheese, in backing industry, and in the extraction of flavor and color compounds from plants. Papain can also be used in forage industry to increase the utilization and transformation rate of proteins and in resolving plant and animal protein to make high health products [113,114]. The potential uses of papain include amino acid esters and peptide synthesis, treatment of acute destructive lactation mastitis, treatment of red blood cells prior to use in antibody-dependent cellmediated cytotoxicity assays with lymphocytes, and enzyme inhibition-based biosensors for food safety and environmental monitoring [115][116][117].…”

Section: Immobilization Of Digestive Enzymes Onto Solid Supportsmentioning

confidence: 99%

Enzyme immobilization: an update

et al. 2013

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Compared to free enzymes in solution, immobilized enzymes are more robust and more resistant to environmental changes. More importantly, the heterogeneity of the immobilized enzyme systems allows an easy recovery of both enzymes and products, multiple re-use of enzymes, continuous operation of enzymatic processes, rapid termination of reactions, and greater variety of bioreactor designs. This paper is a review of the recent literatures on enzyme immobilization by various techniques, the need for immobilization and different applications in industry, covering the last two decades. The most recent papers, patents, and reviews on immobilization strategies and application are reviewed.

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Section: Immobilization Of Digestive Enzymes Onto Solid Supportsmentioning

confidence: 99%

Enzyme immobilization: an update

et al. 2013

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“…Continuous reactors provide high productivities and minimize downstream time, enzyme cost and capital investment (Abraham et al, 2004), and offer an attractive design for enzyme reactors, especially when dealing with unclarified substrate fluids (Roy and Gupta, 2003). The present work had as objective to study immobilization and stabilization of β-galactosidase and application on continuous reactor processing whey as substrate, following research on enzyme isolation and purification (Monti et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Hydrolysis of whey lactose by immobilized β-Galactosidase

Mariotti

Yamanaka

Araújo

et al. 2008

Braz. arch. biol. technol.

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“…Purificación de las proteasas desde el látex con precipitación por sales Utilizando el método modificado de Baines y Brocklehurst (1978) modificado por Monti et al (2000), se procedió de la siguiente manera: Se disolvieron 5,0 g de látex estabilizados con EDTA (1mM pH7) y con buffer acetato de sodio (10 mM a pH5.0) 1:1 w/v, hasta tener un pH 5 teniendo un volumen de 10 mL (M1). La solución de látex M1 fue ajustada hasta pH 9,0 agregándole granallas de NaOH (221465 Sigma-Aldrich), en agitación (agitador magnético Labor MRM LE302, Bulgaria).…”

Section: Extracción Del Látex Vasconcellea Candicansunclassified

“…La separación de cuatro proteasas y no de una sola puede deberse a que no se realizó el ajuste de proteínas del extracto del látex a 65 mg/mL antes del fraccionamiento de sal, como lo sugieren Baines y Brocklehurst (1979). La Fracción A, papaína de "mito", muestra una banda muy nítida a nivel del estándar de papaína de Sigma (Figura 3A, 3B) y según el Rf tiene una masa molecular de 21,0 kDa, dato semejante al obtenido por Monti et al (2000) al purificar papaína de C. papaya en una columna de Sephadex G75.…”

Section: Electroforesis En Gel De Poliacrilamida (12%) Con Sdsunclassified

Purification and preliminary characterization of latex proteases of Vasconcellea candicans (A. Gray) A. DC (Mito)

Gutiérrez¹,

Nolasco²,

Cruz³

2017

sci. agropecu

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ResumenEstudios preliminares indican que, el látex fresco del "Mito" tiene una actividad específica de papaína de 1,84 veces mayor a la encontrada en el látex of papaya, por lo que el objetivo de este trabajo fue purificar y caracterizar las proteasas del látex fresco del "Mito" que tuvieran actividad de papaína. El extracto crudo de proteasas se obtuvo a partir del látex de "Mito" el cual fue resuspendido (1:1) en buffer acetato de Na 10 mM a pH 5,0; inmediatamente se precipitaron proteínas a pH 9,0 y luego con sulfato de amonio al 45%. Posteriormente se purificó en una columna de Sephadex G-100 y se obtuvieron tres fracciones: A, B y C; utilizando como sustrato caseína se midió la actividad enzimática específica (AEE). Se encontró que para la Fracción A la AEE fue de 87,74 nkat.mg -1 proteína, para la Fracción B fue de 14,93 nkat.mg -1 proteína y para la Fracción C fue de 16,13 nkat.mg -1 proteína. La AEE de la fracción A frente a la de papaína de látex fresco de C. papaya fue 13,3 veces mayor. En el análisis electroforético (gel desnaturalizante, 12%) se observa para la fracción A dos bandas de proteínas teniendo una de ellas una "relación de frente" semejante al estándar de papaína. Además, se observó que la fracción A (papaína de "Mito") frente a diferentes concentraciones de caseína, usada como sustrato, presenta una curva sigmoidea michaeliana; a diferentes volúmenes de enzima se muestra un comportamiento lineal; tiene un pH óptimo a 7,5 y es activa hasta 60 ºC.Palabras clave: Lomas de Perú; papaya silvestre; látex; papaína; Vasconcella candicans (A. Gray). AbstractPreliminary studies indicate that, the "Mito" fresh latex, has a specific activity of papain from 1.84 times greater than that found in the latex of papaya, so the objective of this study was to purify and characterize "Mito" fresh latex proteases that have activity of papain. The crude extract protease was obtained from the "Mito" latex which was re-suspended (1:1) in 10 mM Na acetate buffer at pH 5.0; immediately proteins were precipitated at pH 9.0 and then with 45% ammonium sulfate. Subsequently, the proteins were purified on a Sephadex G-100 column and were three fractions: A, B and C. Using as a substrate casein, the enzymatic specific activity (ESA) was measured and was found to be the fraction A was 87.74 nkat.mg -1 protein, for fraction B was 14.93 nkat.mg -1 protein and for fraction C it was 16.13 nkat.mg -1 protein. ESA of fraction A against papain of fresh latex of C. papaya was 13.3 times greater. Electrophoretic analysis (12% denaturant gel) shows for A fraction, two protein bands having one of them a relation similar to the papain standard. In addition, there was observed that the A fraction (papain of "Mito") against different concentrations of casein, used as a substrate, displays a michaeliane sigmoid curve; different volumes of enzyme shows a linear behavior; it has an optimum pH of 7.5 and is active up to 60 °C.

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Purification of papain from fresh latex of Carica papaya

Abstract: In the present study we wish to report a method of crystallizing papain from fresh papaya latex which gave higher yields than previously reported.

Cited by 40 publications

References 16 publications

Enzyme immobilization: an update

Enzyme immobilization: an update

Hydrolysis of whey lactose by immobilized β-Galactosidase

Purification and preliminary characterization of latex proteases of Vasconcellea candicans (A. Gray) A. DC (Mito)

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