Protease—A Versatile and Ecofriendly Biocatalyst with Multi-Industrial Applications: An Updated Review

Naveed, Muhammad; Nadeem, Fareeha; Mehmood, Tahir; Bilal, Muhammad; Anwar, Zahid; Amjad, Fazeeha

doi:10.1007/s10562-020-03316-7

Cited by 132 publications

(70 citation statements)

References 108 publications

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“…Proteases are enzymes that catalyze the hydrolysis of proteins resulting in their breakdown into peptides and amino acids. They represent an important group of industrial enzymes, accounting for almost 60% of the entire enzyme market and 40% of the global enzyme sales [1]. Proteases are in fact used in various industrial sectors, including those of detergents, leather goods, food, fine chemicals, pharmaceuticals, and cosmetics, and can be obtained from different sources such as plants, animal, and microorganisms, with the latter source contributing to nearly two-third of industrially used proteases.…”

Section: Introductionmentioning

confidence: 99%

Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme

Oliveira¹,

Claudino²,

Converti

et al. 2021

Catalysts

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Microbial proteases are commonly produced by submerged (SmF) or solid-state fermentation (SSF), whose combination results in an unconventional method, called sequential fermentation (SF), which has already been used only to produce cellulolytic enzymes. In this context, the aim of the present study was the development of a novel SF method for protease production using wheat bran as a substrate. Moreover, the kinetic and thermodynamic parameters of azocasein hydrolysis were estimated, thus providing a greater understanding of the catalytic reaction. In SF, an approximately 9-fold increase in protease activity was observed compared to the conventional SmF method. Optimization of glucose concentration and medium volume by statistical means allowed us to achieve a maximum protease activity of 180.17 U mL−1. The obtained enzyme had an optimum pH and temperature of 7.0 and 50 °C, respectively. Kinetic and thermodynamic parameters highlighted that such a neutral protease is satisfactorily thermostable at 50 °C, a temperature commonly used in many applications in the food industry. The results obtained suggested not only that SF could be a promising alternative to produce proteases, but also that it could be adapted to produce several other enzymes.

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Section: Introductionmentioning

confidence: 99%

Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme

Oliveira¹,

Claudino²,

Converti

et al. 2021

Catalysts

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“…Several enzymes have been purified partially or completely for therapeutic, biotechnological, and industrial applications, and proteolytic enzymes are extensively used for these purposes [ 1 ]. Proteolytic enzymes catalyze the hydrolysis of peptide bonds in a variety of biological processes.…”

Section: Introductionmentioning

confidence: 99%

“…The enzyme from papaya became the model enzyme of the group known as the papain family. These enzymes have a structure with two main domains: an N -terminal helical domain and a β C-terminal leaf domain, containing the catalytic site with the characteristic cysteine amino acid residues, as well as histidine and asparagine [ 1 , 2 , 3 ]. Cysteine proteases are present in the pineapple-derived enzymatic complex known as bromelain (Bro).…”

Section: Introductionmentioning

confidence: 99%

Collagenase Activity of Bromelain Immobilized at Gold Nanoparticle Interfaces for Therapeutic Applications

et al. 2021

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Bromelain (Bro) is a multiprotein complex extracted from the pineapple plant Ananas comosus, composed of at least eight cysteine proteases. Bro has a wide range of applications in medicine and industry, where the stability of its active proteases is always a major concern. The present study describes the improvement of stability and gain of specific activity in the enzymatic content of Bro immobilized on gold nanoparticles (GNPs). GNPs were synthesized in situ using Bro as the reducing and stabilizing agents and characterized by surface plasmon resonance and transmission electron microscopy. Consistent with the structural changes observed by circular dichroism analysis, the association with GNPs affected enzyme activity. The active Bro immobilized on GNPs (NanoBro) remained stable under storage and gained thermal stability consistent with a thermophilic enzyme. Proteolytic assays were performed on type I collagen membranes using fluorescence spectroscopy of O-phthaldialdehyde (OPA), changes in the membrane superficial structure, and topography by scanning electron microscopy, FTIR, and scanning laser confocal microscopy. Another characteristic of the NanoBro observed was the significant increase in susceptibility to the inhibitory effect of E-64, indicating a gain in cysteine protease activity. The higher stability and specific activity of NanoBro contributed to the broadening and improvement of Bro applications.

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“…The proteolytic enzymes are used in several industrial processes, such as the production of food, pharmaceuticals, as well as in fabric softening, hair removal, and detergent formulation, which is why they lead the world market for sales of enzymes [7,8]. Alkaline proteases, produced from submerged cultivation, have been successfully obtained using a stirred tank-type bioreactor operating in batch [9,10].…”

Section: Introductionmentioning

confidence: 99%

Production, Purification, and Characterization of Extracellular Alkaline Protease From Bacillus Firmus Var. Arosia NCIB 10557

Dias

Silva

Santana

et al. 2021

Preprint

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The most important alkaline proteases from the commercial standpoint are produced by bacteria of the genus Bacillus and used mainly in the formulation of detergents. The aim of the present study was to evaluate the production, partial purification, and characteristics of alkaline protease obtained by Bacillus firmus var. arosia NCIB 10557 in fed-batch fermentation with constant feeding profile and carbon source restriction. Firstly, it was carried out on batch fermentation and after 6.5 h of fermentation, glucose became limiting, and then the fed-batch was started with a flow rate of 0.0802 mL/min. Maximum activity (998.1 U/mL) was reached after 10.5 h of fed-batch, with a subsequent 60.91 % drop in activity after two hours. The purification steps resulted in a 1.65-fold increase in the value of the specific activity. The protease showed optimum activity at 37°C and pH 9 and residual activity above 80 % at pH 11 and 12. Residual activity was greater than 70 % at temperatures ranging from 30 to 70 °C and 90 % of this activity was maintained for 30 minutes at 70 °C until the occurrence of complete inactivation. Enzyme activity was estimated using SDS. The organic solvents Triton X-100, Tween-20, EDTA and β-mercaptoethanol and the ions Zn2+, Fe2+, Cu2+ and Ni2+ partially inhibited the activity of the protease. Ca2+, Mn2+ and Mg2+ had no stimulating action on the enzyme.

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Protease—A Versatile and Ecofriendly Biocatalyst with Multi-Industrial Applications: An Updated Review

Cited by 132 publications

References 108 publications

Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme

Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme

Collagenase Activity of Bromelain Immobilized at Gold Nanoparticle Interfaces for Therapeutic Applications

Production, Purification, and Characterization of Extracellular Alkaline Protease From Bacillus Firmus Var. Arosia NCIB 10557

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