Improvement of tea leaves fermentation through pectinases

Thakur, J. N.; Gupta, Reena

doi:10.1556/amicr.59.2012.3.3

Cited by 13 publications

(1 citation statement)

References 20 publications

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“…Depending on mode of action, pectinases are classified as esterases, depolymerases (hydrolases and lyases), and protopectinases. [1] In varied processes like retting and degumming of plant bast fibers, [2] scouring of cotton, [3] wastewater treatment, [4] papermaking, [5] extraction and clarification of fruit juices, [6] oil extraction, [7] coffee [8] and tea fermentations, [9] production of oligosaccharides as functional food components, [10] extraction of DNA from plants, [11] and others, pectinases find their applications.…”

Section: Introductionmentioning

confidence: 99%

Characterization, Kinetic, and Thermodynamic Studies of Marine Pectinase FromBacillus subtilis

Joshi

Nerurkar

Adivarekar

2014

Preparative Biochemistry and Biotechnology

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Characterization, kinetic and thermodynamic parameters of purified pectinase from Bacillus subtilis, isolated from a marine sediment sample collected from Chinchani beach at Tarapore, India, were studied. Marine pectinase produced under submerged growth conditions was purified by ammonium sulfate precipitation followed by gel filtration chromatography using DEAE cellulose. Partial characterization of the marine pectinase was carried out in terms of effect of pH, temperature, substrate concentration, and metal ions. It was found that pectinase from marine B. subtilis showed maximal activity in alkaline buffer at pH 9.0 and at 40°C. It was also found that metal ions, namely, Mn(2+) and Fe(2+), stimulate pectinase activity. Marine pectinase followed Michaelis-Menten kinetics. The kinetics and thermodynamic parameters of the purified marine pectinase from B. subtilis were studied as the characterization of the enzyme is vital for its use in industrial processes.

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Section: Introductionmentioning

confidence: 99%

Characterization, Kinetic, and Thermodynamic Studies of Marine Pectinase FromBacillus subtilis

Joshi

Nerurkar

Adivarekar

2014

Preparative Biochemistry and Biotechnology

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Pectinases as promising green biocatalysts having broad‐spectrum applications: Recent trends, scope, and relevance

Kaur

Sharma

Joshi

et al. 2023

Biotech and App Biochem

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Pectinases are a collection of multiple enzymes that have a common substrate, that is, pectin. They can act on different parts of pectin due to the structural heterogeneity of pectin. Therefore, they have been placed in different groups, such as protopectinases, polygalacturonases, polymethylesterases, pectin lyases, and pectate lyases. They are naturally present both in multicellular organisms such as higher plants and in unicellular organisms such as microbes. In past decade, it has been witnessed that chemical and mechanical methods employed in industrial processes have led to environmental hazards and serious health disorders, thus increasing the search for eco‐friendly approaches with minimal health risks. Hence, microbial enzymes have been extensively used as safer alternative for these environmentally unsafe methods. Among these microbial enzymes, pectinases hold great significance and is one of the principal enzymes that have been used commercially. It is predominantly used as a green biocatalyst for fruit, fiber, oil, textile, beverage, pulp, and paper industry. Thus, this review focuses on the structure of pectin, microbial sources of pectin, and principle industrial applications of pectinases.

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Immobilization of alkaline polygalacturonate lyase from Bacillus subtilis on the surface of bacterial polyhydroxyalkanoate nano-granules

Ran

Tan

Dai

et al. 2017

Appl Microbiol Biotechnol

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Alkaline polygalacturonate lyase (PGL), one of the pectinolytic enzymes, has been widely used for the bioscouring of cotton fibers, biodegumming, and biopulp production. In our study, PGL from Bacillus subtilis was successfully immobilized on the surface of polyhydroxyalkanoate (PHA) nanogranules by fusing PGL to the N-terminal of PHA synthase from Ralstonia eutropha via a designed linker. The PGL-decorated PHA beads could be simply achieved by recombinant fermentation and consequent centrifugation. The fused PGL occupied 0.985% of the total weight of purified PHA granules, which was identified by mass spectrometer-based quantitative proteomics. The activity of immobilized PGL (184.67 U/mg PGL protein) was a little lower than that of the free PGL (215.93 U/mg PGL protein). The immobilization process did not affect the optimal pH and the optimal temperature of the PGL, but it did enhance the thermostability as well as the pH stability at certain conditions, which will extend the practicability of the immobilized PGL-PHA beads in the alkaline and generally harsh bioscouring process. Furthermore, the immobilized PGL still retained more than 60% of its initial activity after 8 cycles of reuse. Our study provided a novel and promising approach for cost-efficient in vivo PGL immobilization, contributing to wider commercialization of this environmental-friendly biocatalyst.

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Improvement of tea leaves fermentation through pectinases

Cited by 13 publications

References 20 publications

Characterization, Kinetic, and Thermodynamic Studies of Marine Pectinase FromBacillus subtilis

Characterization, Kinetic, and Thermodynamic Studies of Marine Pectinase FromBacillus subtilis

Pectinases as promising green biocatalysts having broad‐spectrum applications: Recent trends, scope, and relevance

Immobilization of alkaline polygalacturonate lyase from Bacillus subtilis on the surface of bacterial polyhydroxyalkanoate nano-granules

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