Search Results Heading

MBRLSearchResults

mbrl.module.common.modules.added.book.to.shelf
Title added to your shelf!
View what I already have on My Shelf.
Oops! Something went wrong.
Oops! Something went wrong.
While trying to add the title to your shelf something went wrong :( Kindly try again later!
Are you sure you want to remove the book from the shelf?
Oops! Something went wrong.
Oops! Something went wrong.
While trying to remove the title from your shelf something went wrong :( Kindly try again later!
    Done
    Filters
    Reset
  • Discipline
      Discipline
      Clear All
      Discipline
  • Is Peer Reviewed
      Is Peer Reviewed
      Clear All
      Is Peer Reviewed
  • Item Type
      Item Type
      Clear All
      Item Type
  • Subject
      Subject
      Clear All
      Subject
  • Year
      Year
      Clear All
      From:
      -
      To:
  • More Filters
      More Filters
      Clear All
      More Filters
      Source
    • Language
2,057 result(s) for "Polygalacturonase"
Sort by:
Pectinase from Microorganisms and Its Industrial Applications
The utilization of microbial pectinase in different industries has been increased in its world demand. The major sources of pectinase are microorganisms mainly bacteria, fungi and yeast. The utilization of low-cost agro-industrial wastes as substrates has been preferable in pectinase production. Pectinase production faced various parameters optimization constraints such as temperature, pH and production times which are the main factors in pectinase production. The pectinase enzyme is getting attention due to its several advantages; hence, it needs to be explored further to take its maximum advantage in different industries. This review discusses the pectin substance structure, substrate for pectinase production, factors influencing pectinase production, the industrial application of microbial pectinase and also discusses challenges and future opportunities of applying microbial pectinase in industry.
Plant immunity triggered by engineered in vivo release of oligogalacturonides, damage-associated molecular patterns
Significance Damage-associated molecular patterns (DAMPs), released from host tissues as a consequence of pathogen attack, have been proposed as endogenous activators of immune responses in both animals and plants. Oligogalacturonides (OGs), oligomers of α-1,4–linked galacturonic acid generated in vitro by the partial hydrolysis of pectin, have been shown to function as potent elicitors of immunity when they are applied exogenously to plant tissues. However, there is no direct evidence that OGs can be produced in vivo or that they function as immune elicitors. This report provides the missing evidence that OGs can be generated in planta and can function as DAMPs in the activation of plant immunity. Oligogalacturonides (OGs) are fragments of pectin that activate plant innate immunity by functioning as damage-associated molecular patterns (DAMPs). We set out to test the hypothesis that OGs are generated in planta by partial inhibition of pathogen-encoded polygalacturonases (PGs). A gene encoding a fungal PG was fused with a gene encoding a plant polygalacturonase-inhibiting protein (PGIP) and expressed in transgenic Arabidopsis plants. We show that expression of the PGIP–PG chimera results in the in vivo production of OGs that can be detected by mass spectrometric analysis. Transgenic plants expressing the chimera under control of a pathogen-inducible promoter are more resistant to the phytopathogens Botrytis cinerea , Pectobacterium carotovorum , and Pseudomonas syringae . These data provide strong evidence for the hypothesis that OGs released in vivo act as a DAMP signal to trigger plant immunity and suggest that controlled release of these molecules upon infection may be a valuable tool to protect plants against infectious diseases. On the other hand, elevated levels of expression of the chimera cause the accumulation of salicylic acid, reduced growth, and eventually lead to plant death, consistent with the current notion that trade-off occurs between growth and defense.
A fungal extracellular effector inactivates plant polygalacturonase-inhibiting protein
Plant pathogens degrade cell wall through secreted polygalacturonases (PGs) during infection. Plants counteract the PGs by producing PG-inhibiting proteins (PGIPs) for protection, reversibly binding fungal PGs, and mitigating their hydrolytic activities. To date, how fungal pathogens specifically overcome PGIP inhibition is unknown. Here, we report an effector, Sclerotinia sclerotiorum PGIP-INactivating Effector 1 (SsPINE1), which directly interacts with and functionally inactivates PGIP. S. sclerotiorum is a necrotrophic fungus that causes stem rot diseases on more than 600 plant species with tissue maceration being the most prominent symptom. SsPINE1 enhances S. sclerotiorum necrotrophic virulence by specifically interacting with host PGIPs to negate their polygalacturonase-inhibiting function via enhanced dissociation of PGIPs from PGs. Targeted deletion of SsPINE1 reduces the fungal virulence. Ectopic expression of SsPINE1 in plant reduces its resistance against S. sclerotiorum . Functional and genomic analyses reveal a conserved virulence mechanism of cognate PINE1 proteins in broad host range necrotrophic fungal pathogens. Plants produce polygalacuturonase-inhibiting proteins (PGIPs) to counteract cell wall degradation by pathogenic microbes. Here the authors show that Sclerotinia sclerotiorum , a fungal pathogen that causes stem rot disease, secretes a PGIP-inactivating effector to diminish plant resistance.
ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE 1 (ADPG1) releases latent defense signals in stems with reduced lignin content
There is considerable interest in engineering plant cell wall components, particularly lignin, to improve forage quality and biomass properties for processing to fuels and bioproducts. However, modifying lignin content and/or composition in transgenic plants through down-regulation of lignin biosynthetic enzymes can induce expression of defense response genes in the absence of biotic or abiotic stress. Arabidopsis thaliana lines with altered lignin through down-regulation of hydroxycinnamoyl CoA:shikimate/quinate hydroxycinnamoyl transferase (HCT) or loss of function of cinnamoyl CoA reductase 1 (CCR1) express a suite of pathogenesisrelated (PR) protein genes. The plants also exhibit extensive cell wall remodeling associated with induction of multiple cell wall-degrading enzymes, a process which renders the corresponding biomass a substrate for growth of the cellulolytic thermophile Caldicellulosiruptor bescii lacking a functional pectinase gene cluster. The cell wall remodeling also results in the release of size- and charge-heterogeneous pectic oligosaccharide elicitors of PR gene expression. Genetic analysis shows that both in planta PR gene expression and release of elicitors are the result of ectopic expression in xylem of the gene ARABIDOPSIS DEHISCENCE ZONE POLYGALACTURONASE 1 (ADPG1), which is normally expressed during anther and silique dehiscence. These data highlight the importance of pectin in cell wall integrity and the value of lignin modification as a tool to interrogate the informational content of plant cell walls.
Genome-wide identification and characterization of polygalacturonase gene family in linseed (Linum usitatissimum L.) and comparative expression in its wild relative (Linum bienne) upon bud fly infestation
Background Linseed is an important minor oilseed crop, which is well known for food, feed, oil, fiber, and pharmaceutical industries. The higher concentrations of omega-3 fatty acid augment their importance. Among the several productivity constraints, the linseed bud fly is a major pest that leads to severe yield loss. Limited donors are available for bud fly resistance, but deeper insight into its characterization at the gene or transcript level is not well studied. Results Identification, characterization, and expression of polygalacturonase encoding genes have been done in the present investigation. A total of 42 LusPG genes were identified in the linseed genome and grouped into two major clades and six subclades. All the genes comprise the Gluco_Hydro_28 domain, whereas two candidates consist of the LRR domain. Three domains, such as “SPNTDG”, “GDDC”, and “CGPGHG”, were found as conserved signatures. The comparative expression in linseed cultivar and one of its wild relatives demonstrated the differential layer of transcriptional regulation modulating bud fly resistance. The gene expression analysis demonstrated that the genes such as Lus10041051 , Lus10043087 , Lus10013025 , and Lus10002727 were found to be significantly regulated upon bud fly infestation. Two candidates, namely Lus10042371 and Lus10026299 , had R-gene domain along with GH28 domain, suggesting their cell wall modification and inhibitor activity. Conclusions The present study identified 42 genes in linseed, with four key genes showing potential for inhibiting bud fly feeding by altering cell walls. These findings provide a foundation for future breeding programs to enhance pest resistance in linseed crops.
PHOTO-SENSITIVE LEAF ROLLING 1 encodes a polygalacturonase that modifies cell wall structure and drought tolerance in rice
• The biosynthesis and modification of cell wall composition and structure are controlled by hundreds of enzymes and have a direct consequence on plant growth and development. However, the majority of these enzymes has not been functionally characterised. • Rice mutants with leaf-rolling phenotypes were screened in a field. Phenotypic analysis under controlled conditions was performed for the selected mutant and the relevant gene was identified by map-based cloning. Cell wall composition was analysed by glycome profiling assay. • We identified a photo-sensitive leaf rolling 1 (psl1) mutant with ‘napping’ (midday depression of photosynthesis) phenotype and reduced growth. The PSL1 gene encodes a cell walllocalised polygalacturonase (PG), a pectin-degrading enzyme. psl1 with a 260-bp deletion in its gene displayed leaf rolling in response to high light intensity and/or low humidity. Biochemical assays revealed PG activity of recombinant PSL1 protein. Significant modifications to cell wall composition in the psl1 mutant compared with the wild-type plants were identified. Such modifications enhanced drought tolerance of the mutant plants by reducing water loss under osmotic stress and drought conditions. • Taken together, PSL1 functions as a PG that modifies cell wall biosynthesis, plant development and drought tolerance in rice.
Fruit softening and pectin disassembly: an overview of nanostructural pectin modifications assessed by atomic force microscopy
BackgroundOne of the main factors that reduce fruit quality and lead to economically important losses is oversoftening. Textural changes during fruit ripening are mainly due to the dissolution of the middle lamella, the reduction of cell-to-cell adhesion and the weakening of parenchyma cell walls as a result of the action of cell wall modifying enzymes. Pectins, major components of fruit cell walls, are extensively modified during ripening. These changes include solubilization, depolymerization and the loss of neutral side chains. Recent evidence in strawberry and apple, fruits with a soft or crisp texture at ripening, suggests that pectin disassembly is a key factor in textural changes. In both these fruits, softening was reduced as result of antisense downregulation of polygalacturonase genes. Changes in pectic polymer size, composition and structure have traditionally been studied by conventional techniques, most of them relying on bulk analysis of a population of polysaccharides, and studies focusing on modifications at the nanostructural level are scarce. Atomic force microscopy (AFM) allows the study of individual polymers at high magnification and with minimal sample preparation; however, AFM has rarely been employed to analyse pectin disassembly during fruit ripening.ScopeIn this review, the main features of the pectin disassembly process during fruit ripening are first discussed, and then the nanostructural characterization of fruit pectins by AFM and its relationship with texture and postharvest fruit shelf life is reviewed. In general, fruit pectins are visualized under AFM as linear chains, a few of which show long branches, and aggregates. Number- and weight-average values obtained from these images are in good agreement with chromatographic analyses. Most AFM studies indicate reductions in the length of individual pectin chains and the frequency of aggregates as the fruits ripen. Pectins extracted with sodium carbonate, supposedly located within the primary cell wall, are the most affected.
Novel Antarctic Endo-Polygalacturonase for Pectin Extraction and Vegetal Tissue Maceration at Mild Temperatures
The aim of the present work was to partially purify and characterize an Antarctic polygalacturonase and to determine the enzyme’s potential in pectin extraction and vegetal maceration at 20 °C. Polygalacturonase was purified by chromatography to obtain an enzymatic preparation of specific activity 30.3 U.mg –1 . Optimal conditions for the polygalacturonase activity were 45 °C and pH 5.0–6.0, and the activation energy for the reaction was 41.8 kJ.mol –1 . Of the enzyme activity, 100% was retained after 3 h at 40 °C. The enzyme was remarkably stable for an hour over a wide range of pH (2.0–12.0). Polygalacturonase activity was slightly reduced in the presence of Ca +2 , Fe +3 , K + , Mn +2 , and Zn +2 , whereas Hg +2 reduced the activity by 60%, suggesting a thiol-dependent catalysis. The apparent molecular weight of the enzyme was 33 kDa. The kinetic constants evaluated against polygalacturonic acid were 0.17 mg.ml –1 (K m ), 480 s –1 (K cat ), and 7.9 µmol.mg –1 .min –1 (V max ). The enzyme was active against different pectic substrates. Thin-layer chromatography revealed an endo -mechanism of action. Polygalacturonase digested lime pomace to aid the extraction of high-methoxylated pectin at 20 °C and increased the vegetal maceration of Capsicum annuum by 24% over the control values.
Optimizing Culture Conditions by Statistical Approach to Enhance Production of Pectinase from Bacillus sp. Y1
It was found that Bacillus sp. Y1 could secrete alkaline pectinase with suitable enzyme system for powerful and fast degumming of ramie fiber. In this study, the medium components and fermentation conditions were optimized by some statistical methods including mixture design, fractional factorial design, central composite design and response surface methodology, and single factor method for enhancing the alkaline pectinase production. The optimized conditions for pectinase production were that the culture was shaken at 34°C for 60 h in 50 mL of medium containing 10.5% (w/v) carbon source (consisting of 3.8% starch, 4.2% wheat bran, and 2.5% sucrose), 0.37% (NH4)2SO4, 0.3% MgSO4, and 0.1% Tween-80, with initial pH 8.2 and inoculation amount of 1.3 mL (with the OD600 of the seed medium about 5.77). Using the optimizing conditions, the activities of polygalacturonate lyase (PGL) and polygalacturonase (PG) in fermentation liquor were increased to 2.00-fold and 3.44-fold, respectively, and the fermentation time shortened 12 hours (from 72 h to 60 h), which showed good application potential in degumming of ramie.
The CIN-TCP transcription factors regulate endocycle progression and pavement cell size by promoting cell wall pectin degradation
In plants, endoreplication, the process where nuclear DNA replicates in the absence of mitosis, and remodeling of the primary cell walls are both coupled with cell expansion. However, the mechanisms by which these two processes coordinate to determine cell size remain largely elusive. Here, employing the tcpΔ7 septuple mutant disabling seven of the eight CIN-TCP transcription factors in Arabidopsis, we find that hindered endoreplication progression in tcpΔ7 whereby ploidy increases from 8 C to beyond is correlated with an increase in cell wall pectin. CIN-TCPs transcriptionally activate POLYGALACTURONASE LIKE 1 ( PGL1 ), which encodes a polygalacturonase downregulating both abundance and molecular mass of pectin polymers. Genetic analysis of PGL1 in both the wild type and tcpΔ7 backgrounds confirm that pectin reduction promotes endocycle progression and cell enlargement. Collectively, these findings reveal a critical role of pectin in regulating endoreplication, providing insights in the understanding of cell growth and organ development in plants. The authors reveal that failure to activate PGL1, a polygalacturonase degrading cell wall pectin, in the tcpΔ7 mutant results in enhanced endoreplication and cell enlargement, unraveling a critical role of pectin in controlling endocycle progression and cell growth.