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Fulltext Direct purification of pectinase from mango (Mangifera Indica Cv. Chokanan) peel using a PEG/salt-based Aqueous Two Phase System

Mehrnoush A, Sarker MZ, Mustafa S, Yazid AM

Molecules, 2011 Oct 10;16(10):8419-27.
PMID: 21986520 DOI: 10.3390/molecules16108419

An Aqueous Two-Phase System (ATPS) was employed for the first time for the separation and purification of pectinase from mango (Mangifera Indica Cv. Chokanan) peel. The effects of different parameters such as molecular weight of the polymer (polyethylene glycol, 2,000-10,000), potassium phosphate composition (12-20%, w/w), system pH (6-9), and addition of different concentrations of neutral salts (0-8%, w/w) on partition behavior of pectinase were investigated. The partition coefficient of the enzyme was decreased by increasing the PEG molecular weight. Additionally, the phase composition showed a significant effect on purification factor and yield of the enzyme. Optimum conditions for purification of pectinase from mango peel were achieved in a 14% PEG 4000-14% potassium phosphate system using 3% (w/w) NaCl addition at pH 7.0. Based on this system, the purification factor of pectinase was increased to 13.2 with a high yield of (97.6%). Thus, this study proves that ATPS can be an inexpensive and effective method for partitioning of pectinase from mango peel.

Matched MeSH terms: Polygalacturonase/isolation & purification*; Polygalacturonase/metabolism*; Polygalacturonase/chemistry
Innovative biocatalyst synthesis of pectinolytic enzymes by cross-linking strategy: Potentially immobilised pectinases for the production of pectic-oligosaccharides from pectin

Abd Rahman NH, Rahman RA, Rahmat Z, Jaafar NR, Puspaningsih NNT, Illias RM

Int J Biol Macromol, 2024 Jan;256(Pt 1):128260.
PMID: 38000618 DOI: 10.1016/j.ijbiomac.2023.128260

Pectinases are outstanding multienzymes, which have the potential to produce new emerging pectic-oligosaccharides (POS) via enzymatic hydrolysis of pectin. However, free pectinase is unable to undergo repeated reaction for the production of POS. This study proposed a sustainable biocatalyst of pectinases known as cross-linked pectinase aggregates (CLPA). Pectinase from Aspergillus aculeatus was successfully precipitated using 2 mg/mL pectinase and 60 % acetone for 20 min at 20 °C, which remained 36.3 % of its initial activity. The prepared CLPA showed the highest activity recovery (85.0 %), under the optimised conditions (0.3 % (v/v) starch and glutaraldehyde mixture (St/Ga), 1.5: 1 of St/Ga, 25 °C, 1.5 h). Furthermore, pectin-degrading enzymes from various sources were used to produce different CLPA. The alteration of pectinase secondary structure gave high stability in acidic condition (pH 4), thermostability, deactivation energy and half-life, and improved storage stability at 4 °C for 30 days. Similarly to their free counterpart, the CLPA exhibited comparable enzymatic reaction kinetics and could be reused eight times with approximately 20 % of its initial activity. The developed CLPA does not only efficaciously produced POS from pectin as their free form, but also exhibited better operational stability and reusability, making it more suitable for POS production.

Matched MeSH terms: Polygalacturonase*
Purification of pectinase from mango (Mangifera indica L. cv. Chokanan) waste using an aqueous organic phase system: a potential low cost source of the enzyme

Amid M, Abdul Manap MY, Mustafa S

J Chromatogr B Analyt Technol Biomed Life Sci, 2013 Jul 15;931:17-22.
PMID: 23770734 DOI: 10.1016/j.jchromb.2013.05.009

As a novel method of purification, an aqueous organic phase system (AOPS) was employed to purify pectinase from mango waste. The effect of different parameters, such as the alcohol concentration (ethanol, 1-propanol, and 2-propanol), the salt type and concentration (ammonium sulfate, potassium phosphate and sodium citrate), the feed stock crude load, the aqueous phase pH and NaCl concentration, were investigated in the recovery of pectinase from mango peel. The partition coefficient (K), selectivity (S), purification factor (PF) and yield (Y, %) were investigated in this study as important parameters for the evaluation of enzyme recovery. The desirable partition efficiency for pectinase purification was achieved in an AOPS of 19% (w/w) ethanol and 22% (w/w) potassium phosphate in the presence of 5% (w/w) NaCl at pH 7.0. Based on the system, the purification factor of pectinase was enhanced 11.7, with a high yield of 97.1%.

Matched MeSH terms: Polygalacturonase/analysis; Polygalacturonase/isolation & purification*; Polygalacturonase/metabolism; Polygalacturonase/chemistry
Fulltext A novel aqueous micellar two-phase system composed of surfactant and sorbitol for purification of pectinase enzyme from Psidium guajava and recycling phase components

Amid M, Murshid FS, Manap MY, Hussin M

Biomed Res Int, 2015;2015:815413.
PMID: 25756051 DOI: 10.1155/2015/815413

A novel aqueous two-phase system composed of a surfactant and sorbitol was employed for the first time to purify pectinase from Psidium guajava. The influences of different parameters, including the type and concentration of the surfactant and the concentration and composition of the surfactant/sorbitol ratio, on the partitioning behavior and recovery of pectinase were investigated. Moreover, the effects of system pH and the crude load on purification fold and the yield of purified pectinase were studied. The experimental results indicated that the pectinase was partitioned into surfactant-rich top phase, and the impurities were partitioned into the sorbitol-rich bottom phase with the novel method involving an ATPS composed of 26% (w/w) Triton X-100 and 23% (w/w) sorbitol at 54.2% of the TLL crude load of 20% (w/w) at pH 6.0. The enzyme was successfully recovered by this method with a high purification factor of 15.2 and a yield of 98.3%, whereas the phase components were also recovered and recycled at rates above 96%. This study demonstrated that this novel ATPS method can be used as an efficient and economical alternative to the traditional ATPS for the purification and recovery of the valuable enzyme.

Matched MeSH terms: Polygalacturonase/isolation & purification*; Polygalacturonase/chemistry*
Fulltext Optimization of extraction of novel pectinase enzyme discovered in red pitaya (Hylocereus polyrhizus) peel

Zohdi NK, Amid M

Molecules, 2013;18(11):14366-80.
PMID: 24264138 DOI: 10.3390/molecules181114366

Plant peels could be a potential source of novel pectinases for use in various industrial applications due to their broad substrate specificity with high stability under extreme conditions. Therefore, the extraction conditions of a novel pectinase enzyme from pitaya peel was optimized in this study. The effect of extraction variables, namely buffer to sample ratio (2:1 to 8:1, X₁), extraction temperature (-15 to +25 °C, X₂) and buffer pH (4.0 to 12.0, X₃) on specific activity, temperature stability, storage stability and surfactant agent stability of pectinase from pitaya peel was investigated. The study demonstrated that the optimum conditions for the extraction of pectinase from pitaya sources could improve the enzymatic characteristics of the enzyme and protect its activity and stability during the extraction procedure. The optimum extraction conditions cause the pectinase to achieve high specific activity (15.31 U/mg), temperature stability (78%), storage stability (88%) and surfactant agent stability (83%). The most desirable conditions to achieve the highest activity and stability of pectinase enzyme from pitaya peel were the use of 5:1 buffer to sample ratio at 5 °C and pH 8.0.

Matched MeSH terms: Polygalacturonase/isolation & purification*
Fulltext Pulp Enhancement of Oil Palm Empty Fruit Bunches (OPEFBs) via Biobleaching by Using Xylano-Pectinolytic Enzymes of Bacillus amyloliquefaciens ADI2

Nawawi MH, Mohamad R, Tahir PM, Asa'ari AZ, Saad WZ

Molecules, 2021 Jul 14;26(14).
PMID: 34299554 DOI: 10.3390/molecules26144279

The present work reports the biobleaching effect on OPEFB pulp upon utilisation of extracellular xylano-pectinolytic enzymes simultaneously yielded from Bacillus amyloliquefaciens ADI2. The impacts of different doses, retention times, pH, and temperatures required for the pulp biobleaching process were delineated accordingly. Here, the OPEFB pulp was subjected to pre-treatment with xylano-pectinolytic enzymes generated from the same alkalo-thermotolerant isolate that yielded those of higher quality. Remarkable enhanced outcomes were observed across varying pulp attributes: for example, enzyme-treated pulp treated to chemical bleaching sequence generated improved brightness of 11.25%. This resulted in 11.25% of less chlorine or chemical consumption required for obtaining pulp with optical attributes identical to those generated via typical chemical bleaching processes. Ultimately, the reduced consumption of chlorine would minimise the organochlorine compounds found in an effluent, resulting in a lowered environmental effect of paper-making processes overall as a consequence. This will undoubtedly facilitate such environmentally-friendly technology incorporation in the paper pulp industry of today.

Matched MeSH terms: Polygalacturonase/metabolism
Fulltext Optimization of freeze drying conditions for purified pectinase from mango (Mangifera indica cv. Chokanan) peel

Mehrnoush A, Mustafa S, Yazid AM

Int J Mol Sci, 2012;13(3):2939-50.
PMID: 22489134 DOI: 10.3390/ijms13032939

Response surface methodology (RSM) along with central composite design (CCD) was applied to optimize the freeze drying conditions for purified pectinase from mango (Mangifera indica cv. Chokanan) peel. The effect of pectinase content (-2.66, 62.66 mg/mL), Arabic gum (-1.21, 10.21%, w/v), and maltodextrin (0.73, 7.26%, w/v) as independent variables on activity, yield, and storage stability of freeze-dried enzyme was evaluated. Storage stability of pectinase was investigated after one week at 4 °C and yield percentage of the enzyme after encapsulation was also determined. The independent variables had the most significant (p < 0.05) effect on pectinase activity and yield of the enzyme. It was observed that the interaction effect of Arabic gum and maltodextrin improved the enzymatic properties of freeze-dried pectinase. The optimal conditions for freeze-dried pectinase from mango peel were obtained using 30 mg/mL of pectinase content, 4.5 (%, w/v) of Arabic gum, and 4 (%, w/v) of maltodextrin. Under these conditions, the maximum activity (11.12 U/mL), yield (86.4%) and storage stability (84.2%) of encapsulated pectinase were achieved.

Matched MeSH terms: Polygalacturonase/isolation & purification*; Polygalacturonase/metabolism
Optimization of ultrasound-assisted extraction of pectinase enzyme from guava (Psidium guajava) peel: Enzyme recovery, specific activity, temperature, and storage stability

Amid M, Murshid FS, Manap MY, Islam Sarker Z

Prep Biochem Biotechnol, 2016;46(1):91-9.
PMID: 25844554 DOI: 10.1080/10826068.2015.1031396

This study aimed to investigate the effects of the ultrasound-assisted extraction conditions on the yield, specific activity, temperature, and storage stability of the pectinase enzyme from guava peel. The ultrasound variables studied were sonication time (10-30 min), ultrasound temperature (30-50 °C), pH (2.0-8.0), and solvent-to-sample ratio (2:1 mL/g to 6:1 mL/g). The main goal was to optimize the ultrasound-assisted extraction conditions to maximize the recovery of pectinase from guava peel with the most desirable enzyme-specific activity and stability. Under the optimum conditions, a high yield (96.2%), good specific activity (18.2 U/mg), temperature stability (88.3%), and storage stability (90.3%) of the extracted enzyme were achieved. The optimal conditions were 20 min sonication time, 40 °C temperature, at pH 5.0, using a 4:1 mL/g solvent-to-sample ratio. The study demonstrated that optimization of ultrasound-assisted process conditions for the enzyme extraction could improve the enzymatic characteristics and yield of the enzyme.

Matched MeSH terms: Polygalacturonase
Betacyanins from Hylocereus polyrhizus: pectinase-assisted extraction and application as a natural food colourant in ice cream

Gengatharan A, Dykes G, Choo WS

J Food Sci Technol, 2021 Apr;58(4):1401-1410.
PMID: 33746268 DOI: 10.1007/s13197-020-04651-8

The effect of solvent, substrate-to-solvent ratio and concentration of pectinase on the extraction of betacyanins from the pulp of red pitahaya (Hylocereus polyrhizus) was evaluated with respect to yield, betacyanin content (BC) and total sugar content. The application of betacyanins from red pitahaya in ice cream was then evaluated by comparison to a commercial colourant, E-162. Without the use of pectinase, the highest yields (9.11 ± 0.35%) of betacyanins were obtained using 95% ethanol at a substrate-to-solvent ratio of 1:1. With the use of pectinase at a concentration of 1.5%, the highest yield (17.11-17.45%) of betacyanins were obtained using water as a solvent at a substrate-to-solvent ratio of 1:1 and 1:2. Pectinase treatment (1.5-2.5%) using water as a solvent yielded betacyanins with the highest BC (126.47-130.83 g kg-1) and lowest total sugar content (57.85-59.74 g kg-1). The BC and total colour changes were similar in ice cream containing betacyanins from red pitahaya and E-162 throughout the 21-days of frozen storage at -18 °C. Betacyanins from red pitahaya or E-162 enhanced the antioxidant properties of ice cream. The sensory evaluation of ice cream containing betacyanins from red pitahaya showed a better colour acceptability than E-162.

Matched MeSH terms: Polygalacturonase
Polygalacturonase production by calcium alginate immobilized Enterobacter aerogenes NBO2 cells

Darah I, Nisha M, Lim SH

Appl Biochem Biotechnol, 2015 Mar;175(5):2629-36.
PMID: 25547814 DOI: 10.1007/s12010-014-1447-4

Bacterial cells of Enterobacter aerogenes NBO2 were entrapped in calcium alginate beads in order to enhance polygalacturonase production compared to free cells. The optimized condition of 5 % (w/v) sodium alginate concentration, agitation speed of 250 rpm, and 15 beads of calcium alginate with inoculum size of 4 % (v/v; 5.4 × 10(7) cells/ml) produced 23.48 U/mL of polygalacturonase compared to free cells of 18.54 U/ml. There was about 26.6 % increment in polygalaturonase production. However, in this study, there was 296.6 % of increment in polygalacturonase production after improvement parameters compared to before improvement parameters of calcium alginate bead immobilization cells (5.92 U/ml). This research has indicated that optimized physical parameters of calcium alginate bead immobilization cells have significantly enhanced the production of polygalacturonase.

Matched MeSH terms: Polygalacturonase/biosynthesis*
A novel liquid/liquid extraction process composed of surfactant and acetonitrile for purification of polygalacturonase enzyme from Durio zibethinus

Amid M, Manap Y, Azmira F, Hussin M, Sarker ZI

J Chromatogr B Analyt Technol Biomed Life Sci, 2015 Jul 1;993-994:1-8.
PMID: 25973865 DOI: 10.1016/j.jchromb.2015.04.034

Polygalacturonase is one of the important enzymes used in various industries such as food, detergent, pharmaceutical, textile, pulp and paper. A novel liquid/liquid extraction process composed of surfactant and acetonitrile was employed for the first time to purify polygalacturonase from Durio zibethinus. The influences of different parameters such as type and concentration of surfactants, concentrations of acetonitrile and composition of surfactant/acetonitrile on partitioning behavior and recovery of polygalacturonase was investigated. Moreover, the effect of pH of system and crude load on purification fold and yield of purified polygalacturonase were studied. The results of the experiment indicated the polygalacturonase was partitioned into surfactant top rich phase with impurities being partitioned into acetonitrile bottom rich phase in the novel method of liquid/liquid process composed of 23% (w/w) Triton X-100 and 19% (w/w) acetonitrile, at 55.6% of TLL (tie line length) crude load of 25% (w/w) at pH 6.0. Recovery and recycling of components also was measured in each successive step of liquid/liquid extraction process. The enzyme was successfully recovered by the method with a high purification factor of 14.3 and yield of 97.3% while phase components were also recovered and recycled above 95%. This study demonstrated that the novel method of liquid/liquid extraction process can be used as an efficient and economical extraction method rather than the traditional methods of extraction for the purification and recovery of the valuable enzyme.

Matched MeSH terms: Polygalacturonase/isolation & purification*
Effects of pectinase clarification treatment on phenolic compounds of pummelo (Citrus grandis l. Osbeck) fruit juice

Shah NN, Rahman RA, Shamsuddin R, Adzahan NM

J Food Sci Technol, 2015 Aug;52(8):5057-65.
PMID: 26243926 DOI: 10.1007/s13197-014-1554-9

The purpose of this study is to investigate the changes occured on phenolic compounds between two Malaysian varieties of pummelo fruit juice: Ledang (PO55) and Tambun (PO52) post-enzymatic clarification. The changes in polyphenols composition were monitored using High Performance Liquid Chromatography Diode Array Detection and Folin Ciocalteu's method. Clarification treatment of pummelo fruit juice with a commercial pectinase was optimized based on incubation temperature, time and enzyme concentration. Both varieties of pummelo fruit juice were treated with different optimized variables which produced the highest clarities with the least effect to the juice physical quality. Tambun variety was found to have significantly more total phenolic compounds (p <0.05) in comparison to Ledang variety, possibly due to the amount of naringin. Three types of hydroxycinnamic acids (chlorogenic, caffeic and coumaric acid) and three compounds of flavanones (naringin, hesperidin and narirutin) were found in both fruit juices, where naringin and chlorogenic acid were the major contributor to the total phenolic content. Naringin, which gave out bitter aftertaste to the juice, was found to decrease, 1.6 and 0.59 % reduction in Ledang and Tambun respectively, post-enzymatic treatment. The decrease in naringin, albeit nominal, could be a potential benefit to the juice production in reducing the bitterness of the juice. Post-enzymatic analysis furthermore resulted in no significance differences (p <0.05) on the total phenolic compounds of both varieties. This study in summary provides a compositional database for Malaysian pummelo fruit juice of various phenolic compounds, which can provide useful information for evaluating the authenticity and the health benefits from the juice.

Matched MeSH terms: Polygalacturonase
Fulltext Partial Purification and Characterisation of Pectinase Produced by Aspergillus niger LFP-1 Grown on Pomelo Peels as a Substrate

Jalil MTM, Ibrahim D

Trop Life Sci Res, 2021 Mar;32(1):1-22.
PMID: 33936548 DOI: 10.21315/tlsr2021.32.1.1

In the present study, pectinase was produced by local fungal isolate, Aspergillus niger LFP-1 grown on pomelo peels as a sole carbon source under solid-state fermentation (SSF). The purification process begins with the concentration of crude enzyme using ammonium sulfate precipitation and followed by purification using anion-exchange column chromatography (DEAE-Sephadex) and subsequently using gel filtration column chromatography (Sephadex G-100). On the other hand, the molecular weight of the purified enzyme was determined through SDS-PAGE. The findings revealed the crude enzyme was purified up to 75.89 folds with a specific activity of 61.54 U/mg and the final yield obtained was 0.01%. The molecular mass of the purified pectinase was 48 kDa. The optimum pH and temperature were 3.5 and 50°C, respectively. This enzyme was stable at a range of pH 3.5 to 4.5 and a relatively high temperature (40°C-50°C) for 100 min. The Km and Vmax were found to be 3.89 mg/mL and 1701 U/mg, respectively. Meanwhile, pectin from citrus fruit and the metal ion (Co2+) were the best substrate and inducer to enhance pectinase yield, respectively.

Matched MeSH terms: Polygalacturonase
Fulltext Cladosporium cladosporioides from the perspectives of medical and biotechnological approaches

AlMatar M, Makky EA

3 Biotech, 2016 Jun;6(1):4.
PMID: 28330073 DOI: 10.1007/s13205-015-0323-4

Fungi are important natural product sources that have enormous potential for the production of novel compounds for use in pharmacology, agricultural applications and industry. Compared with other natural sources such as plants, fungi are highly diverse but understudied. However, research on Cladosporium cladosporioides revealed the existence of bioactive products such as p-methylbenzoic acid, ergosterol peroxide (EP) and calphostin C as well as enzymes including pectin methylesterase (PME), polygalacturonase (PG) and chlorpyrifos hydrolase. p-Methylbenzoic acid has ability to synthesise 1,5-benzodiazepine and its derivatives, polyethylene terephthalate and eicosapentaenoic acid. EP has anticancer, antiangiogenic, antibacterial, anti-oxidative and immunosuppressive properties. Calphostin C inhibits protein kinase C (PKC) by inactivating both PKC-epsilon and PKC-alpha. In addition, calphostin C stimulates apoptosis in WEHI-231 cells and vascular smooth muscle cells. Based on the stimulation of endoplasmic reticulum stress in some types of cancer, calphostin C has also been evaluated as a potential photodynamic therapeutic agent. Methylesterase (PME) and PG have garnered attention because of their usage in the food processing industry and significant physiological function in plants. Chlorpyrifos, a human, animal and plant toxin, can be degraded and eliminated by chlorpyrifos hydrolase.

Matched MeSH terms: Polygalacturonase
Fulltext Insight into plant cell wall degradation and pathogenesis of Ganoderma boninense via comparative genome analysis

Ramzi AB, Che Me ML, Ruslan US, Baharum SN, Nor Muhammad NA

PeerJ, 2019;7:e8065.
PMID: 31879570 DOI: 10.7717/peerj.8065

Background: G. boninense is a hemibiotrophic fungus that infects oil palms (Elaeis guineensis Jacq.) causing basal stem rot (BSR) disease and consequent massive economic losses to the oil palm industry. The pathogenicity of this white-rot fungus has been associated with cell wall degrading enzymes (CWDEs) released during saprophytic and necrotrophic stage of infection of the oil palm host. However, there is a lack of information available on the essentiality of CWDEs in wood-decaying process and pathogenesis of this oil palm pathogen especially at molecular and genome levels.
Methods: In this study, comparative genome analysis was carried out using the G. boninense NJ3 genome to identify and characterize carbohydrate-active enzyme (CAZymes) including CWDE in the fungal genome. Augustus pipeline was employed for gene identification in G. boninense NJ3 and the produced protein sequences were analyzed via dbCAN pipeline and PhiBase 4.5 database annotation for CAZymes and plant-host interaction (PHI) gene analysis, respectively. Comparison of CAZymes from G. boninense NJ3 was made against G. lucidum, a well-studied model Ganoderma sp. and five selected pathogenic fungi for CAZymes characterization. Functional annotation of PHI genes was carried out using Web Gene Ontology Annotation Plot (WEGO) and was used for selecting candidate PHI genes related to cell wall degradation of G. boninense NJ3.
Results: G. boninense was enriched with CAZymes and CWDEs in a similar fashion to G. lucidum that corroborate with the lignocellulolytic abilities of both closely-related fungal strains. The role of polysaccharide and cell wall degrading enzymes in the hemibiotrophic mode of infection of G. boninense was investigated by analyzing the fungal CAZymes with necrotrophic Armillaria solidipes, A. mellea, biotrophic Ustilago maydis, Melampsora larici-populina and hemibiotrophic Moniliophthora perniciosa. Profiles of the selected pathogenic fungi demonstrated that necrotizing pathogens including G. boninense NJ3 exhibited an extensive set of CAZymes as compared to the more CAZymes-limited biotrophic pathogens. Following PHI analysis, several candidate genes including polygalacturonase, endo β-1,3-xylanase, β-glucanase and laccase were identified as potential CWDEs that contribute to the plant host interaction and pathogenesis.
Discussion: This study employed bioinformatics tools for providing a greater understanding of the biological mechanisms underlying the production of CAZymes in G. boninense NJ3. Identification and profiling of the fungal polysaccharide- and lignocellulosic-degrading enzymes would further facilitate in elucidating the infection mechanisms through the production of CWDEs by G. boninense. Identification of CAZymes and CWDE-related PHI genes in G. boninense would serve as the basis for functional studies of genes associated with the fungal virulence and pathogenicity using systems biology and genetic engineering approaches.

Matched MeSH terms: Polygalacturonase
Hormones, polyamines, and cell wall metabolism during oil palm fruit mesocarp development and ripening

Teh HF, Neoh BK, Wong YC, Kwong QB, Ooi TE, Ng TL, et al.

J Agric Food Chem, 2014 Aug 13;62(32):8143-52.
PMID: 25032485 DOI: 10.1021/jf500975h

Oil palm is one of the most productive oil-producing crops and can store up to 90% oil in its fruit mesocarp. Oil palm fruit is a sessile drupe consisting of a fleshy mesocarp from which palm oil is extracted. Biochemical changes in the mesocarp cell walls, polyamines, and hormones at different ripening stages of oil palm fruits were studied, and the relationship between the structural and the biochemical metabolism of oil palm fruits during ripening is discussed. Time-course analysis of the changes in expression of polyamines, hormones, and cell-wall-related genes and metabolites provided insights into the complex processes and interactions involved in fruit development. Overall, a strong reduction in auxin-responsive gene expression was observed from 18 to 22 weeks after pollination. High polyamine concentrations coincided with fruit enlargement during lipid accumulation and latter stages of maturation. The trend of abscisic acid (ABA) concentration was concordant with GA₄ but opposite to the GA₃ profile such that as ABA levels increase the resulting elevated ABA/GA₃ ratio clearly coincides with maturation. Polygalacturonase, expansin, and actin gene expressions were also observed to increase during fruit maturation. The identification of the master regulators of these coordinated processes may allow screening for oil palm variants with altered ripening profiles.

Matched MeSH terms: Polygalacturonase/genetics; Polygalacturonase/metabolism
Fulltext Postharvest analysis of lowland transgenic tomato fruits harboring hpRNAi-ACO1 construct

Behboodian B, Mohd Ali Z, Ismail I, Zainal Z

ScientificWorldJournal, 2012;2012:439870.
PMID: 22919320 DOI: 10.1100/2012/439870

The plant hormone, ethylene, is an important regulator which involved in regulating fruit ripening and flower senescence. In this study, RNA interference (RNAi) technology was employed to silence the genes involved in ethylene biosynthetic pathway. This was achieved by blocking the expression of specific gene encoding the ACC oxidase. Initially, cDNA corresponding to ACO1 of lowland tomato cultivar (MT1), which has high identity with ACO1 of Solanum lycopersicum in GenBank, was cloned through RT-PCR. Using a partial coding region of ACO1, one hpRNAi transformation vector was constructed and expressed ectopically under the 35S promoter. Results showed that transgenic lines harboring the hpRNA-ACO1 construct had lower ethylene production and a longer shelf life of 32 days as compared to 10 days for wild-type fruits. Changes in cell wall degrading enzyme activities were also investigated in cases where the transgenic fruits exhibited reduced rates of firmness loss, which can be associated with a decrease in pectin methylesterase (PME) and polygalacturonase (PG) activities. However, no significant change was detected in both transgenic and wild-type fruits in terms of β-galactosidase (β-Gal) activity and levels of total soluble solid, titratable acid and ascorbic acid.

Matched MeSH terms: Polygalacturonase/metabolism
Fulltext A Review on the Biotechnological Applications of the Operational Group Bacillus amyloliquefaciens

Ngalimat MS, Yahaya RSR, Baharudin MMA, Yaminudin SM, Karim M, Ahmad SA, et al.

Microorganisms, 2021 Mar 17;9(3).
PMID: 33802666 DOI: 10.3390/microorganisms9030614

Bacteria under the operational group Bacillus amyloliquefaciens (OGBa) are all Gram-positive, endospore-forming, and rod-shaped. Taxonomically, the OGBa belongs to the Bacillus subtilis species complex, family Bacillaceae, class Bacilli, and phylum Firmicutes. To date, the OGBa comprises four bacterial species: Bacillus amyloliquefaciens, Bacillus siamensis, Bacillus velezensis and Bacillus nakamurai. They are widely distributed in various niches including soil, plants, food, and water. A resurgence in genome mining has caused an increased focus on the biotechnological applications of bacterial species belonging to the OGBa. The members of OGBa are known as plant growth-promoting bacteria (PGPB) due to their abilities to fix nitrogen, solubilize phosphate, and produce siderophore and phytohormones, as well as antimicrobial compounds. Moreover, they are also reported to produce various enzymes including α-amylase, protease, lipase, cellulase, xylanase, pectinase, aminotransferase, barnase, peroxidase, and laccase. Antimicrobial compounds that able to inhibit the growth of pathogens including non-ribosomal peptides and polyketides are also produced by these bacteria. Within the OGBa, various B. velezensis strains are promising for use as probiotics for animals and fishes. Genome mining has revealed the potential applications of members of OGBa for removing organophosphorus (OPs) pesticides. Thus, this review focused on the applicability of members of OGBa as plant growth promoters, biocontrol agents, probiotics, bioremediation agents, as well as producers of commercial enzymes and antibiotics. Here, the bioformulations and commercial products available based on these bacteria are also highlighted. This review will better facilitate understandings of members of OGBa and their biotechnological applications.

Matched MeSH terms: Polygalacturonase

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