A new Bacillus licheniformis mutant strain producing serine protease efficient for hydrolysis of soy meal proteins

Костылева, Е.В.; Середа, А. С.; Velikoretskaya, I.A.; Nefedova, L. I.; Sharikov, A. Yu.; Tsurikova, N. V.; Lobanov, N. S.; Семенова, М. В.; Sinitsyn, A. P.

doi:10.1134/s0026261716040123

Cited by 9 publications

(5 citation statements)

References 11 publications

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“…Bioengineered enzymes with greater stability are being generated in the detergent industry, especially using rDNA technology. Under extreme conditions, the expression of gene encoding for proteases through using different vector systems including pHY300PLK, pKL9610, pFX1, and plasmid may be maintained and expressed in Bacillus stearothermophilus, B. stearothermophilus, E. coli , and B. subtilis (Roja Rani et al, 2012; Kostyleva et al, 2016).…”

Section: Protease and Yield Improvementmentioning

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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Section: Protease and Yield Improvementmentioning

confidence: 99%

Microbial Proteases Applications

Razzaq

Shamsi

Ali³

et al. 2019

Front. Bioeng. Biotechnol.

423

195

View full text Add to dashboard Cite

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“…It can grow at even higher temperatures, which is helpful for enzymes used in substrate processing at higher temperatures and results in faster reaction rates. Bacillus licheniformis produces a variety of extracellular enzymes, including amylases, cellulases, laccases, and proteases (de Boer et al 1994;Kostyleva et al 2016). Because the bacterium can grow at a higher temperature, the enzymes it produces are naturally thermostable.…”

Section: Introductionmentioning

confidence: 99%

Characterization of moderately thermostable α-amylase-producing Bacillus licheniformis from decaying potatoes and sweet potatoes

Ashraf

Arshad

Rahman

et al. 2018

BioRes

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Bacillus licheniformis is an endospore-forming bacterium that is commonly present in soil. The aim of the present study was to isolate and characterize local strains of α-amylase producing B. licheniformis. Soil samples were collected from the decaying surfaces of potatoes and sweet potatoes. The samples were identified by Gram staining, spore staining, and motility testing under aerobic conditions. Twenty-three isolates were found to be from the Bacillus genus and six of those (26%) were found to be B. licheniformis. Two representative samples were run on API 20E and API 50 CH biochemical kits, and 16S rDNA polymerase chain reaction. The isolates were confirmed to be B. licheniformis by the API-web program and molecular detection. Partially purified α-amylase was characterized to determine the effect of the incubation period, temperature tolerance, and pH stability. The activity peaked at 740 mU/mL after 42 h of culturing. The relative activity reached a maximum at 55 °C and a pH of 8.0. The decaying surfaces of potatoes and sweet potatoes are promising sources of α-amylase-producing strains of B. licheniformis that can tolerate both a high temperature and drastic pH level.

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“…Mutant kGy-04-UV-25 was accordingly selected on the basis of superior improvement from 36,209.54 U (123.73 mg protein) in the parent strain to 85,873.38 U (284.93 mg protein); some 2.3-fold increase in protein yield and 2.37-fold improvement in activity units. Many authors have reported successful improvement of alkaline protease by UV [29] or gamma irradiation [30] , especially in Bacillus species. However, there are only a few reports on combinatorial mutagenesis [31] but none on alternate combinations.…”

Section: Resultsmentioning

confidence: 99%