scholarly journals A partially folded intermediate conformation is induced in pectate lyase C by the addition of 8-anilino-1-naphthalenesulfonate (ANS)

2001 ◽  
Vol 10 (10) ◽  
pp. 2123-2130 ◽  
Author(s):  
Douglas E. Kamen ◽  
Robert W. Woody
Keyword(s):  
Pectate Lyase ◽  
Partially Folded Intermediate

scholarly journals High-CO2 Treatment Prolongs the Postharvest Shelf Life of Strawberry Fruits by Reducing Decay and Cell Wall Degradation

Foods ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1649
Author(s):  
Hyang-Lan Eum ◽  
Seung-Hyun Han ◽  
Eun-Jin Lee
Keyword(s):  
Cell Wall ◽  
Shelf Life ◽  
Physiological Mechanism ◽  
Pectate Lyase ◽  
Pectin Methylesterase ◽  
Cell Wall Degradation ◽  
Cell Wall Degrading Enzymes ◽  
High Co2 ◽  
Genes Encoding ◽  
Co2 Treatment

Improved methods are needed to extend the shelf life of strawberry fruits. The objective of this study was to determine the postharvest physiological mechanism of high-CO2 treatment in strawberries. Harvested strawberries were stored at 10 °C after 3 h of exposure to a treatment with 30% CO2 or air. Pectin and gene expression levels related to cell wall degradation were measured to assess the high-CO2 effects on the cell wall and lipid metabolism. Strawberries subjected to high-CO2 treatment presented higher pectin content and firmness and lower decay than those of control fruits. Genes encoding cell wall-degrading enzymes (pectin methylesterase, polygalacturonase, and pectate lyase) were downregulated after high-CO2 treatment. High-CO2 induced the expression of oligogalacturonides, thereby conferring defense against Botrytis cinerea in strawberry fruits, and lowering the decay incidence at seven days after its inoculation. Our findings suggest that high-CO2 treatment can maintain strawberry quality by reducing decay and cell wall degradation.

scholarly journals Secretion of Anti-Plasmodium Effector Proteins from a Natural Pantoea agglomerans Isolate by Using PelB and HlyA Secretion Signals

2011 ◽  
Vol 77 (13) ◽  
pp. 4669-4675 ◽  
Author(s):  
Dawn C. Bisi ◽  
David J. Lampe
Keyword(s):  
Control Strategies ◽  
Pectate Lyase ◽  
Erwinia Carotovora ◽  
Individual Characteristics ◽  
Pantoea Agglomerans ◽  
Effector Proteins ◽  
World Health ◽  
Content Type ◽  
E Coli ◽  
The Individual

ABSTRACTThe insect-vectored disease malaria is a major world health problem. New control strategies are needed to supplement the current use of insecticides and medications. A genetic approach can be used to inhibit development of malaria parasites (Plasmodiumspp.) in the mosquito host. We hypothesized thatPantoea agglomerans, a bacterial symbiont ofAnophelesmosquitoes, could be engineered to express and secrete anti-Plasmodiumeffector proteins, a strategy termed paratransgenesis. To this end, plasmids that include thepelBorhlyAsecretion signals from the genes of related species (pectate lyase fromErwinia carotovoraand hemolysin A fromEscherichia coli, respectively) were created and tested for their efficacy in secreting known anti-Plasmodiumeffector proteins (SM1, anti-Pbs21, and PLA2) inP. agglomeransandE. coli.P. agglomeranssuccessfully secreted HlyA fusions of anti-Pbs21 and PLA2, and these strains are under evaluation for anti-Plasmodiumactivity in infected mosquitoes. Varied expression and/or secretion of the effector proteins was observed, suggesting that the individual characteristics of a particular effector may require empirical testing of several secretion signals. Importantly, those strains that secreted efficiently grew as well as wild-type strains under laboratory conditions and, thus, may be expected to be competitive with the native microbiota in the environment of the mosquito midgut.

Molecular identification and pectate lyase production by Bacillus strains involved in cocoa fermentation

2011 ◽  
Vol 28 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Honoré G. Ouattara ◽  
Sylvie Reverchon ◽  
Sébastien L. Niamke ◽  
William Nasser
Keyword(s):  
Molecular Identification ◽  
Pectate Lyase ◽  
Cocoa Fermentation ◽  
Bacillus Strains

scholarly journals Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin

Microbiology ◽  
2006 ◽  
Vol 152 (3) ◽  
pp. 617-625 ◽  
Author(s):  
Margarita Soriano ◽  
Pilar Diaz ◽  
Francisco I. Javier Pastor
Keyword(s):  
Bacillus Subtilis ◽  
Pectate Lyase ◽  
Maximum Activity ◽  
Methyl Esterification ◽  
Pectate Lyases ◽  
Action Analysis ◽  
Paenibacillus Barcinonensis ◽  
Esterification Degree ◽  
Micro Organisms ◽  
High Degree

The gene yvpA from Bacillus subtilis was cloned and expressed in Escherichia coli. It encoded a pectate lyase of 221 amino acids that was denominated PelC. The heterologously expressed enzyme was purified by His-tag affinity chromatography and characterized. PelC depolymerized polygalacturonate and pectins of methyl esterification degree from 22 % to 89 %, exhibiting maximum activity on 22 % esterified citrus pectin. It showed an absolute Ca2+ requirement and the optimum temperature and pH were 65 °C and pH 10, respectively. The deduced amino acid sequence of PelC showed 53 % identity to pectate lyase PelA from Paenibacillus barcinonensis, which was also characterized. Similarly to PelC, purified PelA showed activity on polygalacturonate and pectins with a high degree of methyl esterification. The two enzymes cleaved pectic polymers to a mixture of oligogalacturonates, indicating an endo mode of action. Analysis of activity on trigalacturonate showed that PelC cleaved it to galacturonic acid and unsaturated digalacturonate, whereas PelA did not show activity on this substrate. PelC and PelA showed high homology to a few recently identified pectate lyases of family 3 and form with them a cluster of small-sized pectate lyases from non-pathogenic micro-organisms.

scholarly journals Pretreatment of pectic wastewater with pectate lyase from an alkalophilic Bacillus sp.

1988 ◽  
Vol 52 (7) ◽  
pp. 1855-1856 ◽  
Author(s):  
Hiroyuki TANABE ◽  
Yoshinari KOBAYASHI ◽  
Isao AKAMATSU
Keyword(s):  
Pectate Lyase ◽  
Bacillus Sp ◽  
Alkalophilic Bacillus

Comparison of Bio and Eco-technologies with Chemical Methods for Pre-treatment of Flax Fibers: Impact on Fiber Properties

2014 ◽  
Vol 9 (4) ◽  
pp. 155892501400900 ◽  
Author(s):  
Sabela Camano ◽  
Nemeshwaree Behary ◽  
Philippe Vroman ◽  
Christine Campagne
Keyword(s):  
Water Absorption ◽  
Fiber Bundle ◽  
Glass Fibers ◽  
Fiber Surface ◽  
Pectate Lyase ◽  
High Water ◽  
Absorption Capacity ◽  
Water Absorption Capacity ◽  
Flax Fibers ◽  
The Impact

Flax fibers, available as fiber bundles, are commonly used as fiber reinforcement in composite materials as a substitute for glass fibers. Pre-treatments are often necessary for improving fiber-resin adhesion, and also to facilitate fiber elementarization, and to improve fiber ability to be implemented in mechanical processes limiting fiber damages. This paper focuses on the impact of biotechnologies (effect of 2 different enzymes: a pectate lyase and a laccase) and of an ecotechnology (ultrasound with ethanol), compared to classical chemical pre-treatments (using aqueous NaOH and ammonia) on the final flax fiber bundle properties, before and after a carding process. Fiber surface properties (wettability and/or zeta potential values), fiber elementarization and mechanical properties vary with the type of treatment (chemical nature of product and conditions used). Fibers elementarised using pectate lyase and ultrasound/ethanol have a hydrophilic surface and a high water absorption capacity, and are also of highest quality in terms of increased fineness. Treatment with NaOH yields the poorest fiber bundle tenacity. Laccase enzyme yields long thick hydrophobic fibers having very low water absorption capacity, and the most neutral surface charge. Properties of flax fibers can be easily monitored using different pre-treatments resulting in fibers which would be suited for various final applications.

scholarly journals Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase from Paenibacillus polymyxa KF-1: Cloning, Expression and Characterization

Molecules ◽  
2018 ◽  
Vol 23 (11) ◽  
pp. 2774 ◽  
Author(s):  
Yan Zhao ◽  
Ye Yuan ◽  
Xinyu Zhang ◽  
Yumei Li ◽  
Qiang Li ◽  
...  
Keyword(s):  
Textile Industry ◽  
Pectate Lyase ◽  
Paenibacillus Polymyxa ◽  
Polygalacturonic Acid ◽  
Optimal Conditions ◽  
Citrus Pectin ◽  
Plant Fiber ◽  
Polysaccharide Lyase ◽  
Glycosidic Bonds ◽  
Fiber Processing

Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of Paenibacillus polymyxa KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from P. polymyxa KF-1 genomic DNA and expressed in Escherichia coli. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and pI of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The Km, vmax and kcat values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s−1, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (Boehmeria nivea) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing.

scholarly journals Modeling the bioconversion of polysaccharides in a continuous reactor: A case study of the production of oligogalacturonates by Dickeya dadantii

2018 ◽  
Vol 294 (5) ◽  
pp. 1753-1762 ◽  
Author(s):  
Jacques-Alexandre Sepulchre ◽  
Sylvie Reverchon ◽  
Jean-Luc Gouzé ◽  
William Nasser
Keyword(s):  
A Priori ◽  
Pectate Lyase ◽  
Degradation Process ◽  
Continuous Reactor ◽  
Practical Implementation ◽  
Dickeya Dadantii ◽  
Pectate Lyases ◽  
Upper Limit ◽  
Promising Avenue

In the quest for a sustainable economy of the Earth's resources and for renewable sources of energy, a promising avenue is to exploit the vast quantity of polysaccharide molecules contained in green wastes. To that end, the decomposition of pectin appears to be an interesting target because this polymeric carbohydrate is abundant in many fruit pulps and soft vegetables. To quantitatively study this degradation process, here we designed a bioreactor that is continuously fed with de-esterified pectin (PGA). Thanks to the pectate lyases produced by bacteria cultivated in the vessel, the PGA is depolymerized into oligogalacturonates (UGA), which are continuously extracted from the tank. A mathematical model of our system predicted that the conversion efficiency of PGA into UGA increases in a range of coefficients of dilution until reaching an upper limit where the fraction of UGA that is extracted from the bioreactor is maximized. Results from experiments with a continuous reactor hosting a strain of the plant pathogenic bacterium Dickeya dadantii and in which the dilution coefficients were varied quantitatively validated the predictions of our model. A further theoretical analysis of the system enabled an a priori comparison of the efficiency of eight other pectate lyase–producing microorganisms with that of D. dadantii. Our findings suggest that D. dadantii is the most efficient microorganism and therefore the best candidate for a practical implementation of our scheme for the bioproduction of UGA from PGA.

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