About: Microbial Proteases Applications

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Microbial Proteases Applications
Creator	Ali, Arfan Ali, Qurban Ashraf, Muhammad Malik, Arif Razzaq, Abdul Sajjad, Muhammad Shamsi, Sadia Ji, Xiao-Jun Qin, Jiufu
Source	PMC
abstract	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.
has issue date	2019-06-12(xsd:dateTime)
bibo:doi	10.3389/fbioe.2019.00110
bibo:pmid	31263696
has license	cc-by
sha1sum (hex)	dc26c72d4373332c80c9cab18a7e3a8b41211333
schema:url	https://doi.org/10.3389/fbioe.2019.00110
resource representing a document's title	Microbial Proteases Applications
has PubMed Central identifier	PMC6584820
has PubMed identifier	31263696
schema:publication	Front Bioeng Biotechnol
resource representing a document's body	covid:dc26c72d4373332c80c9cab18a7e3a8b41211333#body_text
is schema:about of	named entity 'PROTEASES' named entity 'MICROBIAL' named entity 'APPLICATIONS' named entity 'Applications' named entity 'X-ray' named entity 'range of applications' named entity 'wheat bran' named entity 'Factor XIa' named entity 'food industry' named entity 'proteases' named entity 'pharmaceutical drug' named entity 'molecular-weight' named entity 'detergent' named entity 'microbes' named entity 'biotechnological applications' named entity 'proteases' named entity 'brewing industry' named entity 'proteases' named entity 'hydrolysis' named entity 'pharmaceutical' named entity 'biotechnological' named entity 'proteases' named entity 'fibrinolytic' named entity 'Metallo' named entity 'fibrin' named entity 'endopeptidases' named entity 'outer membrane' named entity 'protein turnover' named entity 'B. subtilis' named entity 'alkaline' named entity 'alginate' named entity 'alkaline' named entity 'proteases' named entity 'bioactive' named entity 'animal cells' named entity 'metalloprotease' named entity 'Ultrafiltration' named entity 'bacterial genome' named entity 'amino acids' named entity 'elastin' named entity 'B. subtilis' named entity 'npr' named entity 'genetic manipulation' named entity 'Penicillium' named entity 'Bacillus' named entity 'N-terminal sequence' named entity 'protein engineering' named entity 'Carlsberg' named entity 'substrate specificity' named entity 'soy sauce' named entity 'proteases' named entity 'sericin' named entity 'proteases' named entity 'substrate' named entity 'Thirumurugan' named entity 'therapeutic agent' named entity 'protease' named entity 'amide' named entity 'protease' named entity 'proteases' named entity 'microbes' named entity 'protease' named entity 'B. subtilis' named entity 'Proteases' named entity 'hydrolyzed' named entity 'gene' named entity 'Shanlin' named entity 'drug discovery' named entity 'structural genes' named entity 'bacteria' named entity 'proteases' named entity 'proteases' named entity 'protease'

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