Enzymatic production of pectic oligosaccharides from polygalacturonic acid with commercial pectinase preparations

Combo, Agnan Marie Michel; Aguedo, Mário; Goffin, Dorothée; Wathelet, Bernard; Paquot, Michel

doi:10.1016/j.fbp.2011.09.003

Cited by 84 publications

(50 citation statements)

References 24 publications

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“…The smallest end product was trigalacturonate, but hexamer seemed to accumulate in the enzyme reaction without further hydrolyzed to the trimer. In contrast, fungal enzymes and commercial enzyme preparations produce mono-, di-, and trigalacturonate as final products (Rexova-Benkova 1970;Armand et al 2000;Combo et al 2012). The present result suggests that the recombinant enzyme might require substrates longer than hexameric to form a productive binding.…”

Section: Bioresourcescommentioning

confidence: 99%

Cloning and Expression of Pectobacterium carotovorum Endo-polygalacturonase Gene in Pichia pastoris for Production of Oligogalacturonates

Rafique

Tabassum

Awan³

et al. 2016

BioResources

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A bacterial endo-polygalacturonase (endo-PGase) gene from the plant pathogen Pectobacterium carotovorum was cloned into pGAPZαA vector and constitutively expressed in Pichia pastoris. The recombinant endoPGase secreted by the Pichia clone showed a 1.7 fold increase when the culture medium included glycerol in replacement of glucose as the carbon source. The enzyme had optimum activity at pH 5.5 and 40 °C with stability between pH 5.0 and 8.0 and at temperatures up to 50 °C. The enzyme activity was enhanced by 41% with the addition of 1 mM Co ++ , and inhibited by Fe ++ with a 63% reduction. The mode of the enzyme action showed internal cleavage of α-1,4 glycoside bonds of polygalacturonic acid and citrus peel pectin. Trigalacturonate and hexagalacturonate were the main hydrolysis products, with a yield of 0.44±0.01 and 0.21±0.01 mg released per mg polygalacturonic acid substrate, respectively. This represents the first report of a microbial endo-PGase that produced trimer and hexamer uniquely as the end products of hydrolysis, in contrast to mixtures of mono-, di-, and trigalacturonates commonly observed for the action of fungal enzymes. Pectic oligosaccharides generated from native carbohydrate polymers offer the potential application as building blocks for value-added products.

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Section: Bioresourcescommentioning

confidence: 99%

Cloning and Expression of Pectobacterium carotovorum Endo-polygalacturonase Gene in Pichia pastoris for Production of Oligogalacturonates

Rafique

Tabassum

Awan³

et al. 2016

BioResources

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“…The non-significant terms were kept when their quadratic or interaction effect showed a significant (p < 0.05) effect on the response variables. The Equations (1)(2)(3)(4) show the main quadratic and interaction effects of the factors affecting the response variables. The estimated regression coefficient of independent variables, as well as R 2 and lack of fit are shown in Table 1.…”

Section: Fitting the Final Reduced Modelsmentioning

confidence: 99%

“…They are of great significance, with a wide range of applications in the fruit and beverage and textile processing industries, in the treatment of pectin wastewaters, degumming of plant fibers, pulp and papermaking, and for coffee and tea fermentation [2]. Most of the commercial production of pectinases is limited to some species of bacteria, yeast and fungi [3]. Due to the extensive applications of the enzyme in various industries there is a need to find novel sources of the enzymes due to their current limited production.…”

Section: Introductionmentioning

confidence: 99%

Optimization of Extraction of Novel Pectinase Enzyme Discovered in Red Pitaya (Hylocereus polyrhizus) Peel

Zohdi

Amid

2013

Molecules

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Plant peels could be a potential source of novel pectinases for use in various industrial applications due to their broad substrate specificity with high stability under extreme conditions. Therefore, the extraction conditions of a novel pectinase enzyme from pitaya peel was optimized in this study. The effect of extraction variables, namely buffer to sample ratio (2:1 to 8:1, X 1 ), extraction temperature (−15 to +25 °C, X 2 ) and buffer pH (4.0 to 12.0, X 3 ) on specific activity, temperature stability, storage stability and surfactant agent stability of pectinase from pitaya peel was investigated. The study demonstrated that the optimum conditions for the extraction of pectinase from pitaya sources could improve the enzymatic characteristics of the enzyme and protect its activity and stability during the extraction procedure. The optimum extraction conditions cause the pectinase to achieve high specific activity (15.31 U/mg), temperature stability (78%), storage stability (88%) and surfactant agent stability (83%). The most desirable conditions to achieve the highest activity and stability of pectinase enzyme from pitaya peel were the use of 5:1 buffer to sample ratio at 5 °C and pH 8.0.

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“…Polygalacturonase and pectin lyase have a great commercial significance in industrial application (Kashyap et al, 2001;Khan et al, 2013;Tu et al, 2013;Kumar and Suneetha, 2014). Whereas most industrial production of pectinases is limited to some species of bacteria, yeast (Gummadi and Panda, 2003;Jayani et al, 2005;Combo et al, 2012). Pectinase enzyme has been the focus of research for many years due to the potential and wide applications in various industrial processes.…”

Section: Issn: 2319-7706 Volume 6 Number 6 (2017) Pp 2729-2739mentioning

confidence: 99%

Partial purification and Characterization of Two Pectinases (Polygalacturonase and Pectin lyase) from Papaya Pericarp (Carica papaya cv. solo 8)

Didier¹,

Hubert²,

Parfait³

et al. 2017

Int.J.Curr.Microbiol.App.Sci

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Enzymatic production of pectic oligosaccharides from polygalacturonic acid with commercial pectinase preparations

Cited by 84 publications

References 24 publications

Cloning and Expression of Pectobacterium carotovorum Endo-polygalacturonase Gene in Pichia pastoris for Production of Oligogalacturonates

Cloning and Expression of Pectobacterium carotovorum Endo-polygalacturonase Gene in Pichia pastoris for Production of Oligogalacturonates

Optimization of Extraction of Novel Pectinase Enzyme Discovered in Red Pitaya (Hylocereus polyrhizus) Peel

Partial purification and Characterization of Two Pectinases (Polygalacturonase and Pectin lyase) from Papaya Pericarp (Carica papaya cv. solo 8)

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