Cloning, expression and characterization of a novel alkaline serine protease gene from native Iranian Bacillus sp.; a producer of protease for use in livestock

Ariyaei, Ahmadreza; Farhadi, Ayoub; Moradian, Fatemeh; Mianji, G. Rahimi

doi:10.1016/j.gene.2019.01.020

Cited by 20 publications

(9 citation statements)

References 26 publications

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“…exhibited stability at wide range, pH 7-10. Similarly, the protease remained stable at 50ºC (Ariyaei et al, 2019). It was reported that extremophilic protease from Pseudomonas aeruginosa showed stability between pH 5 and 8 that was almost 100% of their activity up to 24 hours (Flores-Fernández et al, 2019).…”

Section: Characterization Of Protease Enzymementioning

confidence: 82%

Characterization of Geobacillus stearothermophilus protease for detergent industry

Iqbal¹,

Aftab²,

Afzal³

et al. 2020

Rev.Mex.Ing.Quim.

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Section: Characterization Of Protease Enzymementioning

confidence: 82%

Characterization of Geobacillus stearothermophilus protease for detergent industry

Iqbal¹,

Aftab²,

Afzal³

et al. 2020

Rev.Mex.Ing.Quim.

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“…Primers used for the polymerase chain reaction were forward primer 5′-CGGGATCCCACRAATACTTCAAGYGCTGA-3′ and reverse: 5′-CGGAATTCGCATTGACTCTACCRTTTTTCCA-3′ 19 . The genomic DNA was isolated using a genomic DNA isolation kit according to the instructions of the company (NucleoSpin, Microbial DNA, MACHEREY-NAGEL, Dȕren, Germany).…”

Section: Methodsmentioning

confidence: 99%

Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs

Gurunathan

Huang

Ponnusamy

et al. 2021

Sci Rep

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Microbial secondary metabolites from extreme environments like hydrothermal vents are a promising source for industrial applications. In our study the protease gene from Bacillus cereus obtained from shallow marine hydrothermal vents in the East China Sea was cloned, expressed and purified. The protein sequence of 38 kDa protease SLSP-k was retrieved from mass spectrometry and identified as a subtilisin serine proteinase. The novel SLSP-k is a monomeric protein with 38 amino acid signal peptides being active over wide pH (7–11) and temperature (40–80 °C) ranges, with maximal hydrolytic activities at pH 10 and at 50 °C temperature. The hydrolytic activity is stimulated by Ca2+, Co2+, Mn2+, and DTT. It is inhibited by Fe2+, Cd2+, Cu2+, EDTA, and PMSF. The SLSP-k is stable in anionic, non-anionic detergents, and solvents. The ability to degrade keratin in chicken feather and hair indicates that this enzyme is suitable for the degradation of poultry waste without the loss of nutritionally essential amino acids which otherwise are lost in hydrothermal processing. Therefore, the proteinase is efficient in environmental friendly bioconversion of animal waste into fertilizers or value added products such as secondary animal feedstuffs.

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“…The former degrades predominantly beta casein while the latter degrades alpha S1-, beta-, and K-casein (305), but genetic studies focus more on the P-I-type protease. These protease genes located on plasmids greatly differ in size and genetic organization in different strains (Yamagata et al, 1995; Rao et al, 1998; Helianti et al, 2018; Jeong et al, 2018; Ariyaei et al, 2019).…”

Section: Protease Engineeringmentioning

confidence: 99%

Microbial Proteases Applications

Razzaq

Shamsi

Ali³

et al. 2019

Front. Bioeng. Biotechnol.

423

195

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The use of chemicals around the globe in different industries has increased tremendously, affecting the health of people. The modern world intends to replace these noxious chemicals with environmental friendly products for the betterment of life on the planet. Establishing enzymatic processes in spite of chemical processes has been a prime objective of scientists. Various enzymes, specifically microbial proteases, are the most essentially used in different corporate sectors, such as textile, detergent, leather, feed, waste, and others. Proteases with respect to physiological and commercial roles hold a pivotal position. As they are performing synthetic and degradative functions, proteases are found ubiquitously, such as in plants, animals, and microbes. Among different producers of proteases, Bacillus sp. are mostly commercially exploited microbes for proteases. Proteases are successfully considered as an alternative to chemicals and an eco-friendly indicator for nature or the surroundings. The evolutionary relationship among acidic, neutral, and alkaline proteases has been analyzed based on their protein sequences, but there remains a lack of information that regulates the diversity in their specificity. Researchers are looking for microbial proteases as they can tolerate harsh conditions, ways to prevent autoproteolytic activity, stability in optimum pH, and substrate specificity. The current review focuses on the comparison among different proteases and the current problems faced during production and application at the industrial level. Deciphering these issues would enable us to promote microbial proteases economically and commercially around the world.

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Cloning, expression and characterization of a novel alkaline serine protease gene from native Iranian Bacillus sp.; a producer of protease for use in livestock

Cited by 20 publications

References 26 publications

Characterization of Geobacillus stearothermophilus protease for detergent industry

Characterization of Geobacillus stearothermophilus protease for detergent industry

Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs

Microbial Proteases Applications

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