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Relevant bibliographies by topics / Pectin enzyme

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Journal articles

Academic literature on the topic 'Pectin enzyme'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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Journal articles on the topic "Pectin enzyme"

1

Pedrolli, Danielle Biscaro, and Eleonora Cano Carmona. "Purification and Characterization of a Unique Pectin Lyase from Aspergillus giganteus Able to Release Unsaturated Monogalacturonate during Pectin Degradation." Enzyme Research 2014 (December 31, 2014): 1–7. http://dx.doi.org/10.1155/2014/353915.

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A pectin lyase, named PLIII, was purified to homogeneity from the culture filtrate of Aspergillus giganteus grown in submerged culture containing orange peel waste as carbon source. PLIII was able to digest apple pectin and citrus pectins with different degrees of methyl esterification. Interestingly, the PLIII activity was stimulated in the presence of some divalent cations including Pb2+ and was not significantly affected by Hg2+. Like other pectin lyases, PLIII is stimulated by but is not dependent on Ca2+. The main soluble product released during the degradation of pectic substances promot

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2

Chandrayan, Puja. "Biological Function(s) and Application (s) of Pectin and Pectin Degrading Enzymes." Biosciences, Biotechnology Research Asia 15, no. 1 (2018): 87–100. http://dx.doi.org/10.13005/bbra/2611.

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Pectin is an integral part of plant cell wall and since centuries pectin extracted from plants is widely used in food and fruit juice processing. Moreover, in last half century, the applications have also invaded into many bio-processing applications such as pharmaceutical, bioenergy, textile, paper and tea processing. In these growing industries, the use of pectinases has grown with a significant amount i.e. approximately 10 % of total global enzyme market comes from pectinases. Herein comprehensive analyses of information related to structure and function of pectin in plant cell wall as well

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3

Nakagawa, Tomoyuki, Kaichiro Yamada, Shuki Fujimura, Takashi Ito, Tatsuro Miyaji, and Noboru Tomizuka. "Pectin utilization by the methylotrophic yeast Pichia methanolica." Microbiology 151, no. 6 (2005): 2047–52. http://dx.doi.org/10.1099/mic.0.27895-0.

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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 methanol-metabolizing enzyme activities. On the other hand, P. methanolica has two alcohol oxidase (AOD) genes, MOD1 and MOD2. On growth on pectin, the P. methanolica mod1Δ and mod1Δmod2Δ strains showed a severe defect in the growth yield, although the mod2Δ strain could grow on polygalacturonate to the same extent as the wild-typ

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4

Takasawa, Toshihide, Keiko Sagisaka, Koichi Yagi, et al. "Polygalacturonase isolated from the culture of the psychrophilic fungus Sclerotinia borealis." Canadian Journal of Microbiology 43, no. 5 (1997): 417–24. http://dx.doi.org/10.1139/m97-059.

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A polygalacturonase was isolated from the culture medium of Sclerotinia borealis, a psychrophilic fungus that grows on lawn and wheat seedling under the snow in winter and induces the snow mold disease. Pectic acid was a better substrate of this enzyme than pectin when the activity was determined by measuring the reducing sugar produced. However, when the activity was measured by viscosity change, the viscosity of pectin decreased more rapidly than that of pectic acid. The results of viscosity change apparently indicate that the polygalacturonase catalyzes pectin hydrolysis as an endo-type enz

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5

Widowati, Esti, Ardhea Mustika Sari, and Rokhimah Sudarmi Ningsih. "KOMBINASI ENZIM POLIGALAKTURONASE DAN ENZIM PEKTINESTERASE PADA KLARIFIKASI SARI BUAH NAGA SUPER MERAH (Hylocereus Costaricensis) DALAM PEMBUATAN SIRUP." Jurnal Teknologi Hasil Pertanian 12, no. 1 (2020): 29. http://dx.doi.org/10.20961/jthp.v12i1.37625.

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<em>The aim of this research was to investigated the effect of polygalacturonase enzyme (PG) from Bacillus licheniformis strain GD2a AR2 0.09%, 0.1%, and 0.11% concentration combine with pectinesterase enzyme (PE) from Bacillus licheniformis strain GD2a KK2 0.5%, 1%, and 1.5% concentration on the super red dragon fruit juice calrification in syrup production based in pH, total soluble solids, transmittance, and viscosity. Polygalacturonase enzyme hydrolized the α-1,4- D-glycosidic form galacturonic acid while the pectinesterase enzyme break the metoxyl group of pectin form pectat acid. B

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6

Fissore, E. N., N. M. Ponce, C. A. Stortz, A. M. Rojas, and L. N. Gerschenson. "Characterisation of Fiber Obtained from Pumpkin (cucumis moschata duch.) Mesocarp Through Enzymatic Treatment." Food Science and Technology International 13, no. 2 (2007): 141–51. http://dx.doi.org/10.1177/1082013207077914.

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Cell wall-enriched pumpkin ( Cucumis moschata Duch.) powder was submitted to enzymatic hydrolysis by cellulase or hemicellulase in order to evaluate the performance of these cell wall-degrading enzymes on that substrate. Different enzyme-substrate ratios were evaluated and the effect exerted by the buffer on cell wall polysaccharides. Cellulase produced the release of pectin macromolecules which include homogalacturonans side chains, the rhamnogalacturonan I core and rhamnogalacturonan II, in conjunction with xylogalacturonans. The content of galacturonic acid in product obtained ranged from 5

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7

Leone, G., and J. Van den Heuvel. "Regulation by carbohydrates of the sequential in vitro production of pectic enzymes by Botrytis cinerea." Canadian Journal of Botany 65, no. 10 (1987): 2133–41. http://dx.doi.org/10.1139/b87-294.

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Cultures of Botrytis cinerea in a basal salt medium supplemented with different pectin-related polysaccharides (French bean cell walls; citrus pectin; sodium polygalacturonate) as the only carbon source were examined daily for polygalacturonase activity, type of pectic enzymes present, and mycelial growth. Total polygalacturonase activity and number of enzymes detectable were influenced by type and concentration of the substrate and by the conidial concentration at which the cultures were started. A consistent sequence in the production of pectic enzymes was found. The polygalacturonase PG2 wa

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8

Huang, Cian-Song, Qiao-Lin Li, Diana Lo, Yuh-Tai Wang, and Ming-Chang Wu. "Anti-inflammatory activity of pectic enzyme-treated pectin on lipopolysaccharide-induced RAW 264.7 cells." Journal of Functional Food and Nutraceutical 1, no. 1 (2019): 23–30. http://dx.doi.org/10.33555/jffn.v1i1.14.

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The purpose of this study was to investigate the ability and pathway of the pectic enzyme-treated (PET) pectin to inhibit the inflammation of macrophage RAW 264.7 induced by lipopolysaccharide. Results showed that PET-pectin produced from 1% substrate and 48 h reaction time had the highest antioxidative activity, thus these parameters were used to produce PET-pectin used in this study. PET-pectin showed no cell cytotoxicity to normal macrophage RAW 264.7 and reduce the nitrite secretion from LPS-induced RAW 264.7 by 20%. Finally, the expression of cytokines, including NO synthase (iNOS), nitri

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9

Yuan, Ye, Xin-Yu Zhang, Yan Zhao, Han Zhang, Yi-Fa Zhou, and Juan Gao. "A Novel PL9 Pectate Lyase from Paenibacillus polymyxa KF-1: Cloning, Expression, and Its Application in Pectin Degradation." International Journal of Molecular Sciences 20, no. 12 (2019): 3060. http://dx.doi.org/10.3390/ijms20123060.

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Pectate lyases play an important role in pectin degradation, and therefore are highly useful in the food and textile industries. Here, we report on the cloning of an alkaline pectate lyase gene (pppel9a) from Paenibacillus polymyxa KF-1. The full-length gene (1350 bp) encodes for a 449-residue protein that belongs to the polysaccharide lyase family 9 (PL9). Recombinant PpPel9a produced in Escherichia coli was purified to electrophoretic homogeneity in a single step using Ni2+-NTA affinity chromatography. The enzyme activity of PpPel9a (apparent molecular weight of 45.3 kDa) was found to be opt

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10

Pieczywek, Piotr Mariusz, Justyna Cybulska та Artur Zdunek. "An Atomic Force Microscopy Study on the Effect of β-Galactosidase, α-l-Rhamnosidase and α-l-Arabinofuranosidase on the Structure of Pectin Extracted from Apple Fruit Using Sodium Carbonate". International Journal of Molecular Sciences 21, № 11 (2020): 4064. http://dx.doi.org/10.3390/ijms21114064.

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The enzyme driven changes in plant cell wall structure during fruit ripening result in debranching, depolymerization and solubilization of pectin polysaccharides, which has an effect in terms of the postharvest quality losses in fruit. Atomic force microscopy (AFM) has revealed that diluted alkali soluble pectins (DASP) from fruit and vegetables have an interesting tendency to self-assemble into regular structures. However, the mechanism is not yet fully understood. The current study is aimed at investigating the role of neutral sugars, namely galactose, rhamnose and arabinose in the formation

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