Characterization of a new, recombinant thermo-active subtilisin-like serine protease derived from Shewanella arctica

Qoura, Farah; Kassab, Elias; Reiße, Steven; Antranikian, Garabed; Brück, Thomas

doi:10.1016/j.molcatb.2015.02.015

Cited by 14 publications

(3 citation statements)

References 27 publications

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“…An extracellular protease produced by B. licheniformis RP1 has an optimum temperature 65-70 • C and exhibits remarkable stability and compatibility at temperatures ranging between 40 and 50 • C when experimented with a broad variety of solid detergents that are available commercially. 20 In 2014, a new recombinant subtilisin-like Ser protease isolated from Shewanella arctica, a psychrophilic bacterium, is reported with surprising tolerance to broad range of temperature (0-80 • C) and it exhibits optimum proteolytic activity at 60 • C. 21 There are also a few discoveries of subtilisin like protease found with optimum activity in low temperature otherwise known as cold active protease. A novel cold active subtilisin-like protease isolated from Bacillus sp.…”

Section: Characteristics Of Subtilisin-like Proteasementioning

confidence: 99%

Versatility of subtilisin: A review on structure, characteristics, and applications

Azrin

Ali

Rahman

et al. 2022

Biotech and App Biochem

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Due to its thermostability and high pH compatibility, subtilisin is most known for its role as an additive for detergents in which it is categorized as a serine protease according to MEROPS database. Subtilisin is typically isolated from various bacterial species of the Bacillus genus such as Bacillus subtilis, B. amyloliquefaciens, B. licheniformis, and various other organisms. It is composed of 268-275 amino acid residues and is initially secreted in the precursor form, preprosubtilisin, which is composed of 29-residues signal peptide, 77-residues propeptide, and 275-residues active subtilisin. Subtilisin is known for the presence of high and low affinity calcium binding sites in its structure. Native subtilisin has general properties of thermostability, tolerance to neutral to high pH, broad specificity, and calcium-dependent stability, which contribute to the versatility of subtilisin applicability. Through protein engineering and immobilization technologies, many variants of subtilisin have been generated, which increase the applicability of subtilisin in various industries including detergent, food processing and packaging, synthesis of inhibitory peptides, therapeutic, and waste management applications.

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Section: Characteristics Of Subtilisin-like Proteasementioning

confidence: 99%

Versatility of subtilisin: A review on structure, characteristics, and applications

Azrin

Ali

Rahman

et al. 2022

Biotech and App Biochem

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show abstract

“…Intracellular proteases are isolated from the host cells by rupturing the cells by using a French press. 56 The cell extract is subjected to centrifugation to obtain a clarified cellfree extract. The second step of purification, to remove most of the impurities from the isolated enzyme, is a chromatography technique applied based on charge, size, or binding affinity.…”

Section: Solid-state Fermentationmentioning

confidence: 99%

“…The proteins are eluted by varying the pH, which may change the surface charge depending on the pH, or by increasing the ionic strength of the elution buffer to enhance the affinity of proteins toward the mobile phase. 18,56 The dialyzed filtrate obtained from filtration of the fermentation broth or the cell-free extract can be directly loaded onto an ion-exchange chromatography column. An alkaline protease was purified by a cation-exchange Mono-S Sepharose column by using a concentration gradient (0e500 mM) of NaCl.…”

Section: Solid-state Fermentationmentioning

confidence: 99%

Latest Overview of Proteases: A Review

Kumar¹,

Anjana²,

Poonam³

et al. 2019

AJABS

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INTRODUCTION: Enzymes are macromolecular biological catalysts that accelerate chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrate into different molecules known as product. The first enzyme to be discovered was amylase 1 in which was originally isolated from barley and catalysis the conversion of starch into sugars. Enzymes have been utilized for thousands of year in microbial processes. Microbes & their enzymes have been applied for preparations of wines, beer, cheese and other milk products. The role of enzyme in fermentation process has been known for less than two hundred years. Versatility of protein molecules present in their diverse functioning including catalytic capabilities and structural organization. Enzymes are considered biocatalyst as they are involved in producing these molecules. Both fungal and bacterial species produce these molecules. 2 Protease also known as proteinase or peptidase is an enzyme group which is involved in proteolysis. Proteolysis is the hydrolysis of peptide bonds. Peptide bonds help in formation of polypeptide chain by linking amino acids together. Proteases have industrial uses and include more than 70% of the industrial enzyme. 3 Fungi and bacteria are the major source of production of this enzyme. Proteases are eco-friendly as the sources of production are generally nonpathogenic and non-toxic. 4 Sources of Proteolytic Enzymes: Proteolytic enzymes are produced by all life forms such as plants, animals, and microorganisms.

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Trends in extracellular serine proteases of bacteria as detergent bioadditive: alternate and environmental friendly tool for detergent industry

Salwan

Sharma

2019

Arch Microbiol

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Characterization of a new, recombinant thermo-active subtilisin-like serine protease derived from Shewanella arctica

Cited by 14 publications

References 27 publications

Versatility of subtilisin: A review on structure, characteristics, and applications

Versatility of subtilisin: A review on structure, characteristics, and applications

Latest Overview of Proteases: A Review

Trends in extracellular serine proteases of bacteria as detergent bioadditive: alternate and environmental friendly tool for detergent industry

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