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Proteases in Leather Processing
Published in Devarajan Thangadurai, Jeyabalan Sangeetha, Industrial Biotechnology, 2017
Vasudeo P. Zambare, Smita S. Nilegaonkar
Serine proteases are characterized by the presence of a serine group in their active site. They are numerous and widespread among viruses, bacteria, and eukaryotes, suggesting that they are vital to the organisms. Based on their structural similarities, serine proteases have been grouped into 20 families, which have been further subdivided into six clans with common ancestors (Barett, 1994). The primary structures of the members of four clans, chymotrypsin (SA), subtilisin (SB), carboxypeptidase C (SC), and Escherichia D-Ala-D-Ala peptidase A (SE) are totally unrelated, suggesting that there are at least four separate evolutionary origins for serine proteases. Clans SA, SB, and SC have a common reaction mechanism consisting of a common catalytic triad of the three amino acids – serine (nucleophile), aspartate (electrophile), and histidine (base). Although the geometric orientations of these residues are similar, the protein folds are quite different, forming a typical example of a convergent evolution.
Alpha-Amylase, Protease, Lipase, and High-Fructose Corn Syrup Production
Published in Debabrata Das, Soumya Pandit, Industrial Biotechnology, 2021
Serine proteases are also called serine endopeptidases, which have an active site of an enzyme containing a serine residue. These serine proteases have an efficient role in functioning in the body, ranging from blood clotting, providing immunity, and inflammation to help the digestive system to digest food in both eukaryotes and prokaryotes. Serine protease usually attacks the active site with serine on the peptide bond. Serine proteases have endo- or exopeptidase activity. Most of the serine proteases hydrolyse amides and esters. These enzymes have been efficiently expressed in mammalian, insect, yeast, and bacterial expression systems. Serine proteases are mainly alkaline in nature and active at pH 7.0–11.0 (Krishna, 2011).
FRET Reporter Molecules for Identification of Enzyme Functions
Published in Grunwald Peter, Biocatalysis and Nanotechnology, 2017
Jing Mu, Hao Lun Cheong, Bengang Xing
Serine proteases hold pivotal roles in many physiological processes in our body, which include digestion, apoptosis and immune response. However, dysfunction of the proteases can lead to inflammation, tumor proliferation, invasion and even metastasis (Sloane et al., 2013). Being closely associated with tumor progression, the ability to detect and monitor serine proteases will help have better understanding of its roles thereby develop better cancer treatment.
Structural and functional analysis of broad pH and thermal stable protease from Penicillium aurantiogriseum URM 4622
Published in Preparative Biochemistry & Biotechnology, 2022
José Manoel Wanderley Duarte Neto, Jônatas de Carvalho Silva, Flávia Sousa, Odete Sofia Lopes Gonçalves, Maria Carolina de Albuquerque Wanderley, Bruno Sarmento, Carolina de Albuquerque Lima, Maria Teresa Neves-Petersen, Ana Lúcia Figueiredo Porto
Proteases (EC 3.4.23.18) are a very important class of hydrolases that catalyze the peptide bonds hydrolysis and can be classified according to, e.g. the source (animal, vegetable or microbial), site of action (endo or exopeptidase) and substrate specificity.[1,2] Commercially, these proteases are responsible for 60% of the whole enzyme market and more than 25% of biomolecules produced for industrial application. They are applied in numerous chemical reactions in various industries. Particularly, the alkaline proteases are applied in food, cleaning, textile and leather industries.[3] Also, the industrial request for resistant alkaline proteases presenting favorable properties is driving the search for new enzymes.[4] Serine proteases are commonly produced by fungi and usually present low molecular mass, are active at neutral and alkaline pH and have applications in many industries.[5]
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
The enzyme was inhibited by 43 and 48% in the presence of EDTA which is an inhibitor for metalloproteases by forming chelate with divalent ions found in the active center.[49] Another chemical, phenyl-methyl-sulfonyl fluoride (PMSF) is a specific inhibitor of serine proteases that blocks the serine residue found at the active site.[6,44] This property of PMSF is helpful for the differentiation of serine proteases. PMSF caused 14% and 37% decrease in the activity of protease from Bacillus sp. EBTA6 at 1 and 2.5 mM concentrations, respectively. Moreover, serine proteases require on divalent metal ions like Ca2+ and Mg2+, for the activity and stability of the enzyme.[34] These results confirmed that the protease from Bacillus sp. EBTA6 was a serine protease. Serine proteases are important group of proteolytic enzymes containing a serine residue in the active center.[49]
Atlantic Forest’s and Caatinga’s semiarid soils and their potential as a source for halothermotolerant actinomycetes and proteolytic enzymes
Published in Environmental Technology, 2023
Marghuel A. Vieira Silveira, Saara M. Batista dos Santos, Débora Noma Okamoto, Itamar Soares de Melo, Maria A. Juliano, Jair Ribeiro Chagas, Suzan P. Vasconcellos
The catalytic mechanism of serine proteases consists in the nucleophilic attack of the hydroxyl group of the serine residue to the peptide bond. Serine proteases present in their active site, a catalytic triad that, generally, comprises the amino acids H, S and A; however, different classes of serine may also present other proton donors, combined with the serine residue at the active site, as two H molecules, one H and one G molecule, just a L residue, among others [61,63]. Moreover, it is believed that representative serine proteases, such as trypsin and chymotrypsin, display preference for residues from R, Y and F [38] which corroborates the findings in the present study.