⌈Pectin, Pectinase, and Protopectinase: Production,⌈ Properties, and Applications

Sakai, Taku; Sakamoto, Tatsuji; Hallaert, Johan; Vandamme, Erick

doi:10.1016/s0065-2164(08)70597-5

Cited by 337 publications

(224 citation statements)

References 166 publications

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“…In plants, one of the major sources of methanol is pectin, which is hydrolysed to methanol and polygalacturonate by pectin methylesterase (PME) (Sakai et al, 1993). It has been reported that many methylotrophic yeasts are able to grow on pectic compounds as sole carbon sources (Lee & Komagata, 1980).…”

Section: Introductionmentioning

confidence: 99%

Pectin utilization by the methylotrophic yeast Pichia methanolica

et al. 2005

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The methylotrophic yeast Pichia methanolica was able to grow on pectic compounds, pectin and polygalacturonate, as sole carbon sources. Under the growth conditions used, P. methanolica exhibited increased levels of pectin methylesterase, and pectin-depolymerizing and methanolmetabolizing enzyme activities. On the other hand, P. methanolica has two alcohol oxidase (AOD) genes, MOD1 and MOD2. On growth on pectin, the P. methanolica mod1D and mod1Dmod2D strains showed a severe defect in the growth yield, although the mod2D strain could grow on polygalacturonate to the same extent as the wild-type strain. The expression of MOD1 was detected in pectin-grown cells, but the MOD2-gene expression detected by pectin was much lower than that of MOD1. Moreover, pectin could induce peroxisome proliferation in P. methanolica, like methanol and oleic acid. These findings showed that P. methanolica was able to utilize the methylester moiety of pectin by means of methanol-metabolic enzymes in peroxisomes, and that the functional AOD subunit for pectin utilization was Mod1p in P. methanolica.

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Section: Introductionmentioning

confidence: 99%

Pectin utilization by the methylotrophic yeast Pichia methanolica

et al. 2005

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“…During plant ripening and other developmental processes, as well as during attack by plant pathogens, pectin is degraded by an array of enzymes that can either depolymerize the pectin backbone (polygalacturonases, pectin and pectate lyases) or alter the structure of the intact backbone [pectin acetylesterases and pectin methylesterase (PME)]. PMEs catalyse the hydrolysis of galacturonate (GalA) methyl esters in the backbone, producing pectate, which is vulnerable to the depolymerizing polygalacturonases and pectate lyases [1]. PMEs, produced by numerous plants, bacteria and fungi [2,3], may differ with respect to their pH optima, isoelectric points and the requirement of calcium for activity [2].…”

Section: Introductionmentioning

confidence: 99%

“…Although the results revealed clear differences between the activities of the two enzymes [3], only preliminary conclusions regarding the substrate specificity could be drawn, since the Abbreviations used : DP, degree of polymerization ; ESI-MS/MS, electrospray ionization tandem MS ; GalA, galacturonate ; HPAEC, high-performance anion-exchange chromatography ; MALDI-MS, matrix-assisted laser-desorption ionization-MS ; PME, pectin methylesterase. 1 These authors contributed equally to this work. 2 To whom correspondence should be addressed (e-mail office!algemeen.mgim.wau.nl).…”

Section: Introductionmentioning

confidence: 99%

Tandem mass spectrometric analysis of Aspergillus niger pectin methylesterase: mode of action on fully methyl-esterified oligogalacturonates

Kester¹,

Benen²,

Visser³

et al. 2000

Biochem. J.

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“…Pectinase production has been studied in the following group of microscopic fungal species: Aspergillus, Penicillium, Colletotrichum, Sclerotina, Fusarium, Trichoderma, Verticulum, Sclerotium, Geotrichum [61][62][63][64][65][66] . Among them A. niger was found to be a good producer of commercial 67,68 . Many industrial firms are involved in the commercial production of pectinases used in protoplast isolation whose purity and activity vary from one source to another.…”

Section: Pectinasementioning

confidence: 99%

"Lignocellulose Degrading Enzymes from Fungi and Their Industrial Applications"

2017

IJCRR

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The rich diversity of fungi and diverse range of enzymes produced by them together make researchers to exploit their potential for various industrial applications. Few of the fungal enzymes have already been harnessed and many other are to be explored and brought into use. Recent studies suggested that the lignin degrading fungi can be used in the bioremediation of aromatic hydrocarbons including dioxins, dibenzofuran, aromatic dyes, etc. Employing fungal enzymes for the treatment of pollutants has gained attraction recent days for their selectivity, specificity and eco-friendly nature. Of these enzymes, peroxidases (lignin peroxidase and manganese peroxidase) and laccases are the two major classes of enzymes involved in biodegradation of lignin and recalcitrant xenobiotics. In addition, cellulase and hemicellulase were found to play a role in the management of lignocellulosic wastes. The present review gives a detailed account on the various lignocelluloses degrading enzymes, their fungal sources and their industrial applications.

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⌈Pectin, Pectinase, and Protopectinase: Production,⌈ Properties, and Applications

Cited by 337 publications

References 166 publications

Pectin utilization by the methylotrophic yeast Pichia methanolica

Pectin utilization by the methylotrophic yeast Pichia methanolica

Tandem mass spectrometric analysis of Aspergillus niger pectin methylesterase: mode of action on fully methyl-esterified oligogalacturonates

"Lignocellulose Degrading Enzymes from Fungi and Their Industrial Applications"

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