Understanding the Basis of Occurrence, Biosynthesis, and Implications of Thermostable Alkaline Proteases

Arya, Prashant; Yagnik, Shivani M.; Rajput, Kiransinh N.; Panchal, Rakeshkumar R.; Raval, Vikram H.

doi:10.1007/s12010-021-03701-x

Cited by 18 publications

(3 citation statements)

References 151 publications

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“…Most characteristics, including pH, temperature, active-site specificity, substrate specificity, catalytic activity, and stability profiles, tend to vary depending on the protease source. Proteases can be classified based on their optimal pH range, which includes acidic (pH 2-6), neutral (pH 7) and alkaline (pH 8-13) (Arya et al, 2021). Alkaline proteases have attracted considerable attention, accounting for approximately 89% of the protease market (Akhter et al, 2024).…”

Section: Introductionmentioning

confidence: 99%

Production of Alkaline Protease by a Novel Anaerobic Bacterium Isolated From a Municipal Anaerobic Treatment System

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Dönmez,

Avcı

2024

Gıda

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In this study, alkaline protease enzyme production by a bacterial strain isolated from sludge samples collected from an anaerobic treatment system was investigated. According to the 16S rDNA sequence analysis, the isolate was identified as Thermoanaerobacter thermohydrosulfuricus (98.52%). Enzyme activity analyses revealed an optimum pH value of 10, an incubation time of 64 h, and a temperature of 35°C. Arabinose and casein hydrolysates were found to be the best carbon and nitrogen sources, respectively. Maximum protease activity was recorded (864.68 U/mL) when arabinose was used instead of glucose. Moreover, the addition of 1 g/L MgSO4.7H2O and 0.25 g/L Tween-80 to the medium increased the enzyme activity. Therefore, it can be concluded that T. thermohydrosulfuricus is a significant producer of alkaline protease enzymes in the culture medium. To the best of our knowledge, this is the first study to investigate the optimization of alkaline protease production by T. thermohydrosulfuricus.

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Section: Introductionmentioning

confidence: 99%

Production of Alkaline Protease by a Novel Anaerobic Bacterium Isolated From a Municipal Anaerobic Treatment System

Sayın Börekçi,

Dönmez,

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2024

Gıda

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“…In industrial processes, fungal proteases are the choice of enzymes over bacterial enzymes as they can be produced using low–cost substrate coupled with high and rapid productivity ( Naeem et al, 2022 ). One more advantage of fungi over bacteria is biomass separation from production media; the mycelia can be easily removed from the broth, simplifying downstream processes ( Souza et al, 2015 ; Arya et al, 2021 ). Therefore, the demand for fungal proteases for their extensive applications in various industries is increasing worldwide.…”

Section: Introductionmentioning

confidence: 99%

Fungal alkaline proteases and their potential applications in different industries

Pawar

Singh

2023

Front. Microbiol.

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The consumption of various enzymes in industrial applications around the world has increased immensely. Nowadays, industries are more focused on incorporating microbial enzymes in multiple processes to avoid the hazardous effects of chemicals. Among these commercially exploited enzymes, proteases are the most abundantly used enzymes in different industries. Numerous bacterial alkaline proteases have been studied widely and are commercially available; however, fungi exhibit a broader variety of proteases than bacteria. Additionally, since fungi are often recognized as generally regarded as safe (GRAS), using them as enzyme producers is safer than using bacteria. Fungal alkaline proteases are appealing models for industrial use because of their distinct spectrum of action and enormous diversity in terms of being active under alkaline range of pH. Unlike bacteria, fungi are less studied for alkaline protease production. Moreover, group of fungi growing at alkaline pH has remained unexplored for their capability for the production of commercially valuable products that are stable at alkaline pH. The current review focuses on the detailed classification of proteases, the production of alkaline proteases from different fungi by fermentation (submerged and solid–state), and their potential applications in detergent, leather, food, pharmaceutical industries along with their important role in silk degumming, waste management and silver recovery processes. Furthermore, the promising role of alkali–tolerant and alkaliphilic fungi in enzyme production has been discussed briefly. This will highlight the need for more research on fungi growing at alkaline pH and their biotechnological potential.

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“…One of the major challenges of incorporating enzymes into bioremediation processes is their limited ability to tolerate harsh pH, ionic force, temperature, and environmental conditions [ 22 ]. Under such conditions, enzymes tend to exhibit a significant loss of activity mainly due to substantial conformational changes that result in active site disruption [ 23 ].…”

Section: Introductionmentioning

confidence: 99%

Comparison of Acetaminophen Degradation by Laccases Immobilized by Two Different Methods via a Continuous Flow Microreactor Process Scheme

Sotelo

Ornelas‐Soto

et al. 2022

Membranes

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The presence of micropollutants in wastewater is one of the most significant environmental challenges. Particularly, pollutants such as pharmaceutical residues present high stability and resistance to conventional physicochemical and biological degradation processes. Thus, we aimed at immobilizing a laccase enzyme by two different methods: the first one was based on producing alginate-laccase microcapsules through a droplet-based microfluidic system; the second one was based on covalent binding of the laccase molecules on aluminum oxide (Al2O3) pellets. Immobilization efficiencies approached 92.18% and 98.22%, respectively. Laccase immobilized by the two different methods were packed into continuous flow microreactors to evaluate the degradation efficiency of acetaminophen present in artificial wastewater. After cyclic operation, enzyme losses were found to be up to 75 µg/mL and 66 µg/mL per operation cycle, with a maximum acetaminophen removal of 72% and 15% and a retention time of 30 min, for the laccase-alginate microcapsules and laccase-Al2O3 pellets, respectively. The superior catalytic performance of laccase-alginate microcapsules was attributed to their higher porosity, which enhances retention and, consequently, increased the chances for more substrate–enzyme interactions. Finally, phytotoxicity of the treated water was lower than that of the untreated wastewater, especially when using laccase immobilized in alginate microcapsules. Future work will be dedicated to elucidating the routes for scaling-up and optimizing the process to assure profitability.

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Understanding the Basis of Occurrence, Biosynthesis, and Implications of Thermostable Alkaline Proteases

Cited by 18 publications

References 151 publications

Production of Alkaline Protease by a Novel Anaerobic Bacterium Isolated From a Municipal Anaerobic Treatment System

Production of Alkaline Protease by a Novel Anaerobic Bacterium Isolated From a Municipal Anaerobic Treatment System

Fungal alkaline proteases and their potential applications in different industries

Comparison of Acetaminophen Degradation by Laccases Immobilized by Two Different Methods via a Continuous Flow Microreactor Process Scheme

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