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Health Monitoring and Pandemic Detection Using IoT and Wireless Communication Technologies
Published in Prashant Ranjan, Ram Shringar Rao, Krishna Kumar, Pankaj Sharma, Wireless Communication, 2023
Prashant Ranjan, Ram Shringar Rao, Krishna Kumar, Pankaj Sharma
Coronaviruses are a major family of viruses. Many coronaviruses, ranging from the common cold to more severe diseases such as Middle East Respiratory Syndrome (MERS) and Serious Acute Respiratory Syndrome (SARS), are known to cause respiratory infections in humans. The newest coronavirus was found to cause coronavirus disease COVID-19. Scientists carried out the first room-temperature X-ray experiments on the primary protease SARS-CoV-2. The virus that causes the COVID-19 disease reproduces by expressing long protein chains that the protease enzyme needs to cut to smaller lengths. Protease is a type of enzyme that separates proteins into lesser proteins or smaller protein units. The protein is shaped like a heart but it’s the heart of the virus that makes it replicate and spread. Figure 4.1 shows a common and well-known structure of a COVID-19 virus.
An Overview of Protease Inhibitors
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Veena Sreedharan, K.V. Bhaskara Rao
Proteases are seen in prokaryotes, fungi and animals and are very necessary for their survival. Proteases are enzymes that help to break down proteins in a method known as proteolysis. Such enzymes are present in a wide range of biological activities, from small protein digestion to extremely controlled cascades. Protease, like hormones, antibodies, and other enzymes, shows a vital physiological part in determining the life span of other proteins. In the physiology of organisms, this is one of the profligated “switching on” and “switching off” regulating systems. Proteases are secreted by a variety of bacteria to break the protein–peptide link into simple small monomers. As a result of multiple clinical trials suggesting their benefits in cancer studies include inflammations, immune regulations and blood flow control, their usage in medicine is garnering more and more attention. Many parasites are involved in pathogenesis, which includes parasite relocation through the host tissue barrier, hemoglobin and blood protein breakdown, immunological invasions, and inflammatory activation. Proteases thus show a decisive part in pathogenesis. Wild action, on the other hand, has negative consequences in the human body. These enzymes found within cancer cells have the ability to break other strong cell wall and membrane, allowing them to spread and grow into additional cell organ and part of the body, resulting in spread from one site to another (Figure 19.1).
Extremophilic Microbes and their Extremozymes for Industry and Allied Sectors
Published in Ajar Nath Yadav, Ali Asghar Rastegari, Neelam Yadav, Microbiomes of Extreme Environments, 2021
Hiran Kanti Santra, Debdulal Banerjee
Proteases are useful in industries such as detergents, degumming of silks, food and feed industry, de-hairing of leathers, cosmetics and pharmaceuticals. They are widely used as washing powders and automatic dishwashing detergents for the degradation of proteinaceous stains caused by blood, milk, egg, grass and also sauces. Gupta et al. (2002) reported the use of subtilopeptidase as an optical lens cleaner. Other commercial proteases of use in several industrial processes are: Alkazym (Novodan, Copenhagen, Denmark), Tergazyme (Alconox, New York, USA), Ultrasil (Henkel, Dusseldorf, Germany) and P3-paradigm (Henkel-Ecolab, Dusseldorf, Germany)—these are of importance in the membrane-cleaning process and other enzymes are prepared for the same purpose. Pronod 153L is made to remove stain of bloods on surgical instruments. Another example of thermophile protease in the detergent industry is alcalase, a serine endopeptidase with optimal activity at 60°C and pH 8.3 (Biotex) obtained from alkalitolerant bacteria Bacillus licheniformis (Maurer 2004). Halophilic protease also remains stable in organic solvents and this uniqueness has made them a valuable tool for their use in the detergent industry. Some halophiles with protease as their extremozyme are Bacillus sp. EMB9 (Sinha and Khare 2013), Geomicrobium sp. EMB2 (Karan and Khare 2010) or Virgibacillus sp. EMB13 (Sinha and Khare 2012).
Efficient three phase partitioning of actinidin from kiwifruit (Actinidia deliciosa) and its characterization
Published in Preparative Biochemistry & Biotechnology, 2023
Bunty Maskey, Dhan Bahadur Karki
Proteases are the enzymes that hydrolyze peptide bonds, and are major type of enzymes that represent about 60% of commercialized enzymes in the world.[1] Protease derived from plant sources can be used to make cheese, tenderize meat, produce bioactive peptides, and alter flour.[2] Having higher catalytic activities, plant proteases can clot milk at a variety of pH and temperature levels.[3] Some plants shown to have proteases that provide good milk coagulating activity are Cynara scolymus,[4]Zingiber officinale,[5,6]Moringa oleifera,[7]Helianthus annuus,[8]Ananas comosus,[9]Carica papaya,[10,11]Wrightia tinctoria,[12]Solanum dubium,[13]Ficus palmata,[14] and Calotropis gigantea.[15]
Characterization and application of a crude bacterial protease to produce antioxidant hydrolysates from whey protein
Published in Preparative Biochemistry & Biotechnology, 2023
Andréia Monique Lermen, Naiara Jacinta Clerici, Dienefer Borchartt Maciel, Daniel Joner Daroit
Proteases are employed by the food, feed, textile, leather, and detergent industries, among others.[3,4] Considering food technology, proteases are used, for instance, as milk-clotting enzymes in cheese production, in baking to modify gluten, as meat tenderization agents, in the reduction of food protein allergy, and to modulate the techno-functional properties of food proteins. The preparation of protein hydrolysates is also focused from food science and health perspectives since, in addition to increments in nutritional value, protein hydrolysates generated through biocatalysis might display various biological activities, which are attributed to peptides released during the proteolytic cleavage of precursor proteins.[5,6] In this sense, diverse plant and animal proteins are investigated to obtain bioactive hydrolysates and peptides.[7,8]
Production, properties and some applications of protease from alkaliphilic Bacillus sp. EBTA6
Published in Preparative Biochemistry & Biotechnology, 2021
Ayşe Avcı, Selin Demir, Fikriye Alev Akçay
Proteases are the hydrolytic enzymes existing in all living organisms that carry out the splitting of proteins into peptides and amino acids.[1] They are useful tools in the industry for a broad range of applications such as stain removal in detergents, silver recovery from X-ray films, dehairing of leathers, milk coagulation in cheese making.[2] Currently, proteases are the most commercialized enzymes which share for around 60% of the global enzyme market and the demand is increasing continuously.[3] Hence, researches on the development of proteases by using protein engineering techniques or on finding the novel ones with specific properties are paid attention to fulfill the requirements.[4,5] Even though plants and animals could be the sources to obtain proteases for industrial purposes, microorganisms are much preferred due to easy and faster production, availability, stability, ease of downstream processing and the fact that production is not affected by climatic conditions.[2,6]