Emerging trends on the role of recombinant pectinolytic enzymes in industries- an overview

Ahmed, Jebin; Thakur, Abhijeet; Goyal, Arun

doi:10.1016/j.bcab.2021.102200

Cited by 18 publications

(4 citation statements)

References 111 publications

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“…According to Shrestha et al (2021), pectinase represents 25% of the world enzyme market, since and its use in the preparation of alcoholic fermented products, such as wine, has been reported for over 200 years. Pectinase is an enzyme responsible for hydrolyzing pectic substances, thereby breaking down the pectin complex into D-galacturonic acids (Ahmed et al, 2021), and its production can have different origins. However, the production of pectinase of microbial origin shows the best productivity rates (John et al, 2020).…”

Section: Profile Of Patents Related To the Production Of Fruit Vinegarsmentioning

confidence: 99%

The role of fruit vinegar in food science: perspectives among consumers, the scientific community and patent holders

Wanderley,

Ferreira,

Nunes

et al. 2023

Biotechnol. Res. Innov.

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Section: Profile Of Patents Related To the Production Of Fruit Vinegarsmentioning

confidence: 99%

The role of fruit vinegar in food science: perspectives among consumers, the scientific community and patent holders

Wanderley,

Ferreira,

Nunes

et al. 2023

Biotechnol. Res. Innov.

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“…Polygalacturonases, pectin lyase, and pectin methyl esterase are enzymes that hydrolyze the glycosidic bonds in pectic substances (Jayani et al 2010; Khatri et al 2015; Wang et al 2015). Polygalacturonase is a depolymerizing enzyme that catalyses the − 1,4 glycosidic linkage in the pectin chain, resulting in galacturonic acid units (Ahmed et al 2021).…”

Section: Introductionmentioning

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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“…It is a type of heteropolysaccharide with weak acidity and strong heat resistance, mainly composed of galacturonic acid, rhamnose, galactose, and arabinose ( Yadav et al, 2009 ; Amin et al, 2019 ). Pectin participates in the cross-linking of cellulose, hemicellulose and lignin rendering the plant tissue structure firm and hindering the invasion of pathogenic microorganisms ( Ahmed et al, 2021 ).…”

Section: Introductionmentioning

confidence: 99%

Improvement of optimum pH and specific activity of pectate lyase from Bacillus RN.1 using loop replacement

Wei

et al. 2023

Front. Bioeng. Biotechnol.

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Background: Alkaline pectate lyase plays an important role in papermaking, biological refining and wastewater treatment, but its industrial applications are largely limited owing to its low activity and poor alkali resistance.Methods: The alkaline pectate lyase BspPel from Bacillus RN.1 was heterologously expressed in Escherichia coli BL21 (DE3) and its activity and alkali resistance were improved by loop replacement. Simultaneously, the effect of R260 on enzyme alkaline tolerance was also explored.Results: Recombinant pectate lyase (BspPel-th) showed the highest activity at 60°C and pH 11.0, and showed significant stability over a wide pH range (3.0–11.0). The specific enzyme activity after purification was 139.4 U/mg, which was 4.4 times higher than that of the wild-type enzyme. BspPel-th has good affinity for apple pectin, since the Vmax and Km were 29 μmol/min. mL and 0.46 mol/L, respectively. Molecular dynamics simulation results showed that the flexibility of the loop region of BspPel-th was improved.Conclusion: The modified BspPel-th has considerable potential for industrial applications with high pH processes.

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Emerging trends on the role of recombinant pectinolytic enzymes in industries- an overview

Cited by 18 publications

References 111 publications

The role of fruit vinegar in food science: perspectives among consumers, the scientific community and patent holders

The role of fruit vinegar in food science: perspectives among consumers, the scientific community and patent holders

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

Improvement of optimum pH and specific activity of pectate lyase from Bacillus RN.1 using loop replacement

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