Enzymatic Maceration of Vegetables with Protopectinases

Nakamura, Takashi; Hours, Roque Alberto; Sakai, Taku

doi:10.1111/j.1365-2621.1995.tb09805.x

Cited by 35 publications

(31 citation statements)

References 22 publications

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“…In this study, we observed significant differences in pectinase, carboxymethyl cellulase, and proteinase activities among the different B. sorokiniana isolates; such enzymes are often associated with initial phases of host penetration. Polysaccharide-degrading enzymes, such as carboxymethyl cellulase and pectin lyase, are commonly involved in the degradation of plant cell walls (NAKAMURA et al 1995, SANCHEZ-ROMERO et al 1998. Indeed, cellulases from B. sorokiniana effectively hydrolyse cellulosic materials, including wheat tissues (GEIMBA et al 1999).…”

Section: Discussionmentioning

confidence: 99%

Extracellular enzymatic activities of Bipolaris sorokiniana isolates

Geimba

Brandelli

2002

J. Basic Microbiol.

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Section: Discussionmentioning

confidence: 99%

Extracellular enzymatic activities of Bipolaris sorokiniana isolates

Geimba

Brandelli

2002

J. Basic Microbiol.

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“…Pectinolytic enzymes are widely used in the food and beverage industries to clarify fruit juices and wines, to improve cloud stability in fruit and vegetable nectars, and to increase the protein content of fruit juices. The ability to degrade pectins could be used as an alternative method of pectin extraction from by-products of the fruit industry and also to macerate vegetable tissues in order to produce single-cell foods [18].…”

Section: Introductionmentioning

confidence: 99%

Production of heterologous polygalacturonase I from Aspergillus kawachii in Saccharomyces cerevisiae in batch and fed-batch cultures

Rojas

Ortiz

Baruque

et al. 2010

J Ind Microbiol Biotechnol

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The pg1 gene from the filamentous fungus Aspergillus kawachii, which codifies for an acid polygalacturonase, was cloned into the pYES2 expression vector, giving rise to the pYES2:pg1ΔI construct. Engineered Saccharomyces cerevisiae, transformed with pYES2:pg1ΔI construct, both expressed and exported an active polygalacturonase with a MW of ~60 kDa and an isoelectric point of 3.7, similar to those reported for the wild-type enzyme. The recombinant enzyme has the ability to hydrolyze polygalacturonic acid at pH 2.5. Heterologous PG1 production was studied under controlled conditions in batch and fed-batch systems. A simultaneous addition of glucose and galactose was found to be the most suitable feeding strategy assayed, resulting in a final PG1 production of 50 U/ml. The production process proposed in this study could be applied for the industrial production of a novel and useful polygalacturonase.

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“…The name PPase for this enzyme was proposed by Sakai et al [1] to differentiate it from the classical polygalacturonases without pectin releasing activity. PPase-SE is highly efficient for enzymatic extraction of pectin from citrus peel [3] and for maceration of potato tissues to obtain single-cell foods [4].…”

Section: Introductionmentioning

confidence: 99%