Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications

Kumari, Megha; Padhi, Srichandan; Sharma, Swati; Phukon, Loreni Chiring; Singh, Sudhir P.; Kumar, Amit

doi:10.1007/s13205-021-03008-y

Cited by 23 publications

(9 citation statements)

References 180 publications

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“…The current tendency is to utilize cold-active enzymes to lower the temperature of industrial processes, allowing for energy savings and reduced carbon footprint, as well as the productive capacity that operate better at ambient or lower temperatures 32 – 34 . Because they are (i) cost-effective, (ii) energy saving, (iii) capable of catalyzing processes without additional heat aid, and (iv) selectively inactivated by mild heat input 35 . In biotechnology, cold-active enzymes are used to prevent a range of unwanted reactions and restrict the loss of volatile components 36 – 39 .…”

Section: Introductionmentioning

confidence: 99%

Production of cold-active pectinases by three novel Cladosporium species isolated from Egypt and application of the most active enzyme

Moharram

Zohri

Hesham

et al. 2022

Sci Rep

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Cladosporium parasphaerospermum, Cladosporium chlamydosporigenum, and Cladosporium compactisporum have all been discovered and characterized as new Cladosporium species. The three new species seemed to generate cold-active pectinases with high activity at pH 6.0 and 10 °C, pH 6.0 and 15 °C, and pH 5.0 and 15 °C, respectively, with the most active being C. parasphaerospermum pectinase. In submerged fermentation (SmF), C. parasphaerospermum produced the most cold-active pectinase with the highest activity and specific activity (28.84 U/mL and 3797 U/mg) after 8 days. C. parasphaerospermum cold-active pectinase was isolated using DEAE-Cellulose anion exchange resin and a Sephadex G 100 gel filtration column. The enzyme was purified 214.4-fold and 406.4-fold greater than the fermentation medium using DEAE-cellulose and Sephadex G 100, respectively. At pH 7.0 and 10 °C, pure pectinase had the highest activity (6684 U/mg), with Km and Vmax determined to be 26.625 mg/mL and 312.5 U/min, respectively. At 5 mM/mL, EDTA, MgCl2, and SDS inhibited the activity of pure pectinase by 99.21, 96.03, and 94.45%, respectively. The addition of 10 U/mL pure pectinase enhanced the yield of apple, orange, apricot, and peach juice by 17, 20, 13, and 24%, respectively, and improved the clarity and colour of orange juice by 194 and 339%, respectively. We can now add cold-active pectinase production to the long list of Cladosporium species that have been identified. We also report three new species that can be used in biotechnological solutions as active microbial pectinase producers. Although further research is needed, these distinct species might be used to decompose difficult and resistant pertinacious wastes as well as clear fruit juices.

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Section: Introductionmentioning

confidence: 99%

Production of cold-active pectinases by three novel Cladosporium species isolated from Egypt and application of the most active enzyme

Moharram

Zohri

Hesham

et al. 2022

Sci Rep

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“…Psychrophilic ß -galactosidases can also be used in valorization of whey, a side-product of cheese production. Hydrolysis of whey by ß -galactosidase produces glucose- and galactose-rich syrups that can be used as sweeteners ( Kumari et al, 2021 ). ß -galactosidases also have transglycosylation activity, where hydrolysis of lactose is accompanied by formation of tri- and tetra saccharides, which, in addition to being low calorie sweeteners, have potential use as prebiotics as they enhance growth of Bifidobacteria in the intestine ( Benešová et al, 2005 ).…”

Section: Extremozymesmentioning

confidence: 99%

“…32bc ( Mangiagalli and Lotti 2021 ). Most of the psychrophilic ß -galactosidases reported originate from the Antarctic and Arctic, and are active over a broad temperature range, from 4–50°C ( Kumari et al, 2021 ). The archaeon Halorubrum lacusprofundi produces a ß -galactosidase active from −5–60°C ( Karan et al, 2013 ).…”

Section: Extremozymesmentioning

confidence: 99%

Industrial Biotechnology Based on Enzymes From Extreme Environments

Mesbah

2022

Front. Bioeng. Biotechnol.

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Biocatalysis is crucial for a green, sustainable, biobased economy, and this has driven major advances in biotechnology and biocatalysis over the past 2 decades. There are numerous benefits to biocatalysis, including increased selectivity and specificity, reduced operating costs and lower toxicity, all of which result in lower environmental impact of industrial processes. Most enzymes available commercially are active and stable under a narrow range of conditions, and quickly lose activity at extremes of ion concentration, temperature, pH, pressure, and solvent concentrations. Extremophilic microorganisms thrive under extreme conditions and produce robust enzymes with higher activity and stability under unconventional circumstances. The number of extremophilic enzymes, or extremozymes, currently available are insufficient to meet growing industrial demand. This is in part due to difficulty in cultivation of extremophiles in a laboratory setting. This review will present an overview of extremozymes and their biotechnological applications. Culture-independent and genomic-based methods for study of extremozymes will be presented.

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“…Previous studies have shown that the flexible protein structure of psychrophilic enzymes was likely damaged during enzyme processing; thus, the commercial application of these reported psychrophilic xylosidases were limited by their poor thermostability and low specific activity [ 4 ]. To overcome this disadvantage, one strategies is to continuously isolate more psychrophilic xylosidases from the natural environment and gene databases, but this is still labor and time consuming, as well as full of uncertainty [ 13 ]. Instead of enzyme mining, desired enzymes can be generated by enzyme engineering based on the relationship between protein structure and function [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

“…It has generally been assumed that mesophilic and thermophilic enzymes have a tendency to be more rigid, whereas psychrophilic enzymes are associated with structure flexibility [ 4 ]. Compared with mesophilic and thermophilic enzymes, psychrophilic enzymes subtly adjust their amino acid composition, e.g., by increasing the content of glycine, reducing the content of proline and arginine, and developing loop regions [ 13 , 14 , 15 , 16 , 17 ]. For example, the ratios of proline and arginine in cold-active valine dehydrogenase from Cytophaga sp.…”

Section: Introductionmentioning

confidence: 99%

Improving the Specific Activity and Thermostability of Psychrophilic Xylosidase AX543 by Comparative Mutagenesis

Pan

Liu

Zhang

et al. 2022

Foods

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Improving the specific activity and thermostability of psychrophilic xylosidase is important for improving its enzymatic performance and promoting its industrial application. Herein, a psychrophilic xylosidase AX543 exhibited activity in the temperature range between 0 and 35 °C, with optimum activity at 20 °C, which is lower than that of other reported psychrophilic xylosidases. The thermostability, specific activity, and catalytic efficiency of the site-directed variants G110S, Q201R, and L2 were significantly enhanced, without affecting the optimal reaction temperature. Comparative protein structural analysis and molecular dynamics simulation indicated that these improvements might be the result of the increased hydrogen bonds interaction and improved structural rigidity. Furthermore, homologous module substitution with four segments demonstrated that the psychrophilic characteristics of AX543 are the results of the whole protein structure, and the C-terminal segment A4 appears to be more essential in determining psychrophilic characteristics, exhibiting potentiality to produce more psychrophilic xylosidases. This study provides valuable structural information on psychrophilic xylosidases and also offers attractive modification strategies to modify catalytic activity, thermostability, and optimal reaction temperature.

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Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications

Cited by 23 publications

References 180 publications

Production of cold-active pectinases by three novel Cladosporium species isolated from Egypt and application of the most active enzyme

Production of cold-active pectinases by three novel Cladosporium species isolated from Egypt and application of the most active enzyme

Industrial Biotechnology Based on Enzymes From Extreme Environments

Improving the Specific Activity and Thermostability of Psychrophilic Xylosidase AX543 by Comparative Mutagenesis

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