Structural and Biochemical Properties of Pectinases

Gummadi, Sathyanarayana N.; Manoj, Narayanan; Kumar, D. Sunil

doi:10.1007/1-4020-5377-0_7

Cited by 27 publications

(14 citation statements)

References 74 publications

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“…These results are of interest not only because of the implication of PGU1 in the molecular dialogue of plant and biotrophic pathogen but also because of the potential industrial applications of pectinolytic enzymes .…”

Section: Discussionmentioning

confidence: 99%

Analysis of a polygalacturonase gene of Ustilago maydis and characterization of the encoded enzyme

Domínguez

González-Hernández

Polaina

et al. 2013

J. Basic Microbiol.

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Ustilago maydis is a pathogenic fungus that produces the corn smut. It is a biotrophic parasite that depends on living plant tissues for its proliferation and development. Polygalacturonases are secreted by pathogens to solubilize the plant cell-wall and are required for pathogen virulence. In this paper, we report the isolation of a U. maydis polygalacturonase gene (Pgu1) and the functional and structural characterization of the encoded enzyme. The U. maydis Pgu1 gene is expressed when the fungus is grown in liquid culture media containing different carbon sources. In plant tissue, the expression increased as a function of incubation time. Pgu1 gene expression was detected during plant infection around 10 days post-infection with U. maydis FB-D12 strain in combination with teliospore formation. Synthesis and secretion of active recombinant PGU1 were achieved using Pichia pastoris, the purified enzyme had a optimum temperature of 34 °C, optimum pH of 4.5, a Km of 57.84 g/L for polygalacturonic acid, and a Vmax of 28.9 µg/min mg. Structural models of PGU1 based on homologous enzymes yielded a typical right-handed β-helix fold of pectinolytic enzymes classified in the glycosyl hydrolases family 28, and the U. maydis PGU1 is related with endo rather than exo polygalacturonases.

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Section: Discussionmentioning

confidence: 99%

Analysis of a polygalacturonase gene of Ustilago maydis and characterization of the encoded enzyme

Domínguez

González-Hernández

Polaina

et al. 2013

J. Basic Microbiol.

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“…It comprises 2 incomplete N-terminal coils contributing to PB2 and PB3, and 12 complete coils up to the very C-terminus of the enzyme. So far, GH28 enzymes have been found displaying 7-10 complete coils [4]. Second, in the last three coils of Tm ExoPG, the b-strands contribute to more than one sheet (green coils in Fig.…”

Section: Overall Structurementioning

confidence: 98%

“…Pectin contains homogalacturonan and rhamnogalacturonan regions, which may be methylated, acetylated or glycosylated by various carbohydrates. Because of the complexity of pectin, its degradation requires an array of depolymerases and esterases [3,4]. Polygalacturonases (PGs) are depolymerases that cleave the backbone glycosidic linkages of pectin using a hydrolytic reaction type.…”

Section: Introductionmentioning

confidence: 99%

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The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer

et al. 2009

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a b s t r a c tThe exopolygalacturonase from Thermotoga maritima is the most thermoactive and thermostable pectinase known to date. Here we present its crystal structure at 2.05 Å resolution. High structural homology around the active site allowed us to propose a model for substrate binding, explaining the exo-cleavage activity and specificity for non-methylated saturated galacturonate at the non-reducing end. Furthermore, the structure reveals unique features that contribute to the formation of stable tetramers in solution. Such an oligomerization has not been observed before for polygalacturonases.

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“…Among the food enzymes pectinases are the complex and diverse group of enzymes that degrade the pectic substances (Gummadi et al, 2007). Pectin and other pectic substances are complex polysaccharides playing an important role in the firmness of plant tissues.…”

Section: Introductionmentioning

confidence: 99%

Bioconversion of wheat bran for polygalacturonase production by Aspergillus sojae in tray type solid-state fermentation

Demi̇r

Tarı

2016

International Biodeterioration & Biodegradation

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a b s t r a c tWheat bran was tested as the solid substrate for the tray-type solid-state fermentation (SSF) production of polygalacturonase (PG) enzyme by A. sojae mutant strain e a high-PG activity producer. PG production of A. sojae was found to reduce as the thickness of the substrate increase from 8 mm to 14 mm at 90% relative humidity. An interaction between the thickness of the bed and relative humidity of the environment was determined with the help of experimental design and statistical analysis tools. As a result, the PG activity could be enhanced by 31% as the process conditions optimized. Additionally, 11 mm thickness and 70% relative humidity were selected as the PG production favoring conditions with the maximum PG activity of 298 U/g substrate in tray type of SSF without the addition of any nutritive or inducing supplements into wheat bran. The kinetic study conducted in the trays revealed the presence of reduction in the water activity on the 4th day of the SSF process under stated conditions. The productivity of the process conducted under optimized conditions was 3.41 U/g substrate À1 h À1 for the 4th day of the SSF.

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Structural and Biochemical Properties of Pectinases

Cited by 27 publications

References 74 publications

Analysis of a polygalacturonase gene of Ustilago maydis and characterization of the encoded enzyme

Analysis of a polygalacturonase gene of Ustilago maydis and characterization of the encoded enzyme

The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer

Bioconversion of wheat bran for polygalacturonase production by Aspergillus sojae in tray type solid-state fermentation

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