Partial Purification and Kinetic Properties of Polygalacturonase from Solanum macrocarpum L. Fruit

Chinedu, Shalom Nwodo; Dayo-Odukoya, Omolola Peace; Iheagwam, Franklyn Nonso

doi:10.3923/biotech.2017.27.33

Cited by 10 publications

(4 citation statements)

References 4 publications

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“…Since pectin is one of the polysaccharides present in the plant cell wall, and with the cell wall being accountable for the structural integrity of the cell, hence it can be suggested that, the significant pectinase activity in the fruit peels of T. daniellii fruit peels in comparison to its leaves, was an indication of the higher pectin (substrate) content in the fruit peels compared to its leaves for the induction of the enzyme secretion from the microorganism [5,48]. Meanwhile, pectin is the substrate required for the fungi's secretion of pectinases such as polygalacturonases [12,49]. As a result, pectin, the substrate for pectinase production, may have been more abundant in orange peels than in the agricultural wastes studied in Figure 2.…”

Section: Resultsmentioning

confidence: 99%

Pectinase Activities of Selected Fungi Grown on Agrowastes via Solid-state Fermentation

Ametefe

Lemo²,

Orji³

et al. 2022

IOP Conf. Ser.: Earth Environ. Sci.

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Pectinases accelerate the breakdown of the glycosidic bonds in pectin into simpler forms. Pectinases in the study were produced using three extraction solvents, three fungi, and six substrates. Citrate buffer, distilled water and 0.1 M NaCl were utilized as extraction solvents. Penicillium sp, Pichia kudriavzevii F2-T429-5 and Aspergillus niger were selectively isolated from the environment and identified. The substrates include; wheat bran, banana peels, orange peels, corn cobs, Thaumatococcus daniellii (sweet prayer plant) fruit peels, and leaves in solid-state fermentation. The dinitro salicylic acid (DNS) technique was used to determine pectinase activity. In comparison to distilled water, the study found that extracting the enzyme from the fermentation medium with 0.1 M NaCl solvent resulted in considerable (p<0.05) activity. The best substrate and fungus were orange peels and Aspergillus niger, respectively. In general, when compared to the yeast Pichia kudriavzevii F2-T429-5, the molds (Penicillium sp. and Aspergillus niger) produced pectinases with higher activity. Orange peel resulted in pectinase production with significant (p<0.05) activity compared to wheat bran, banana peels, corn cobs, Thaumatococcus daniellii (sweet prayer plant) fruit peels, and leaves. Additionally, Pichia kudriavzevii F2-T429-5 in Thaumatococcus daniellii fruit peel fermentation produced pectinase with the lowest activity. The inference drawn from the study shows the potential of T. daniellii fruit peels, its leaves, and Pichia kudriavzevii F2-T429-5 for pectinase production.

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Section: Resultsmentioning

confidence: 99%

Pectinase Activities of Selected Fungi Grown on Agrowastes via Solid-state Fermentation

Ametefe

Lemo²,

Orji³

et al. 2022

IOP Conf. Ser.: Earth Environ. Sci.

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“…As Km is the substrate concentration at which the enzyme is active, therefore, the pectin enzyme produced was active at 0.3620 mg/ml of substrate concentration [14]. The equation of the Lineweaver-Burk plot was obtained as y = 0.0824x + 0.2276 with R² of 0.9685.…”

Section: Resultsmentioning

confidence: 99%

“…Different factors such as temperature, pH, substrate concentration has been shown by studies to in uence the properties of enzymes [4,8,14]. In fruit processing, the performance of pectinase signi cantly affects the outcome or quality of product and processes such as yield and turbidity, thereby, leading to enhancement of the clari cation process.…”

Section: Introductionmentioning

confidence: 99%

Effect of Characterized Pectinase Produced From Aspergillus Niger on the Clarification of Orange and Pineapple Juices

Ametefe

Oluwadamilare

Ibidapo

et al. 2021

Preprint

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Background: Owing to the importance of enzyme in fruit processing, demand in quality pectinase has increased. As a result, understanding the properties of locally produced pectinase is very important to encourage promotion in its application in the industry. In this study, Aspergillus niger was isolated, screened for its ability to secrete pectinase. The screened Aspergillus niger was used to produce pectinase using solid state fermentation of orange peels. Results: The effect of temperature and its stability, pH and its stability, substrate concentration, metal ions (Na+, Ca2+, Mg2+, K+, Mn2+, Zn2+, Co2+, and Fe2) were also investigated. The characterized pectinase was applied in the clarification of both orange and pineapple juices. The findings revealed that the enzyme was most effective at 50oC and relatively stable at 20oC activity of about 0.50 mg/ml for both. The optimal pH of 5 at about 0.50 mg/ml, and stabilized pH of 4 with approximately similar activity was also obtained. Of the metals ions investigated, Na+ gave the highest activity of about 0.61 mg/ml compared to ethylenediamine tetraacetic acid (EDTA) which displayed an inhibitory effect. On further optimizing for the concentration of Na+, low concentration of the ion (10 mM) had higher activity of about 0.61 mg/ml. The (Km) and Vmax was about 0.36 mg/ml and 4.39 U/ml. Conclusion: The characterized pectinase clarified both orange and pineapple juices, with enhanced clarification in orange juice compared to pineapple juice. Therefore, the characterized crude pectinase was suitable for application in the clarification of juices.

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“…Ammonium sulphate precipitation increased the enzyme's speci c activity from 6.89 U/mg to 12.42 U/mg. Polygalacturonase can be precipitated with 0-90% ammonium sulphate depending on the source of the enzyme (Mohammed et al, 2010;Shalom et al, 2017). Second, the sample was analyzed on two columns of chromatography, the rst of which yielded 2.93 mg/ml of protein produced from 80 mL enzyme extract and puri ed 3.58 folds by Sephadex G -200, and the second of which yielded speci c activity of 24.66 U/mL.…”

Section: Enzyme Puri Cationmentioning

confidence: 99%

Isolation and Characterization of polygalacturonase producing thermophilic Aspergillus spp. isolated from decayed tomato fruits

Sinshaw,

2024

Preprint

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In this study, a polygalacturonase-producing fungus was isolated from decaying tomatoes. Based on colony morphology and hyphal characteristics, this fungus has been identified as Aspergillus sp. The fungus was used in solid-state fermentation to produce an acidic polygalacturonase enzyme. The crude extract obtained from solid-state fermentation had an activity of 94.6 U/mL. The enzyme was then purified using ammonium sulphate precipitation and column chromatography. Ammonium sulphate precipitation increased the enzyme's specific activity from 6.89 U/mg to 12.42 U/mg. Sephadex G-200 was used to purify the enzyme 3.58 times, and its specific activity was determined to be 24.66 U/mg. The Sephacryl S-100 column was responsible for achieving a final fold purification of 9.93 and a specific activity of 68.41 U/mg. When polygalacturonic acid was used as a substrate, the purified enzyme showed the best performance. The enzyme's optimum temperature and pH were found to be 55°C and 5, respectively. CaCl2 was found to be the best chelating ion for the enzyme. This enzyme is recommended for use in a variety of industrial applications.

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Partial Purification and Kinetic Properties of Polygalacturonase from Solanum macrocarpum L. Fruit

Cited by 10 publications

References 4 publications

Pectinase Activities of Selected Fungi Grown on Agrowastes via Solid-state Fermentation

Pectinase Activities of Selected Fungi Grown on Agrowastes via Solid-state Fermentation

Effect of Characterized Pectinase Produced From Aspergillus Niger on the Clarification of Orange and Pineapple Juices

Isolation and Characterization of polygalacturonase producing thermophilic Aspergillus spp. isolated from decayed tomato fruits

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