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Marine Algal Secondary Metabolites Are a Potential Pharmaceutical Resource for Human Society Developments
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Somasundaram Ambiga, Raja Suja Pandian, Lazarus Vijune Lawrence, Arjun Pandian, Ramu Arun Kumar, Bakrudeen Ali Ahmed Abdul
Proteases enzymes, commonly known as biological catalysts, are responsible for a wide range of biochemical processes. They’ve been used in a variety of fields, especially therapeutics. The properties of molecules produced from the marine differ from those of their terrestrial counterparts. Marine microbes (epibionts and endosymbionts), which are abundant in unique environments, produce a plethora of medically and industrially essential molecules. These microbes secrete enzymes with specific characteristics like pH, metal, heat and cryo-tolerance and so on. Proteases are enzymes that break down lengthy chains of proteins into smaller fragments. Endopeptidases and exopeptidases are the two large families of proteases depending on their method of action. Exopeptidases degrade terminal amino acid positions attached to polypeptide chains, while endopeptidases catalyze the breakdown of peptide bonds in the middle portion of polypeptide chains. A further way of classifying proteases is by their optimum pH, which might be neutral, acidic, or alkaline. In terms of the active centers involved, enzymes can be classed as cysteine proteases, metalloproteases, serine proteases and aspartyl proteases.
Nature’s Green Catalyst for Environmental Remediation, Clean Energy Production, and Sustainable Development
Published in Miguel A. Esteso, Ana Cristina Faria Ribeiro, A. K. Haghi, Chemistry and Chemical Engineering for Sustainable Development, 2020
Benny Thomas, Divya Mathew, K. S. Devaky
Proteases are class of enzymes responsible for the hydrolysis and reverse synthesis of peptide bonds in aqueous environment and nonaqueous environment, respectively.52 They hydrolyze the proteinaceous substance produced by shedding and molting of appendages, death of animals, and as the by-product of poultry, fishery, leather, detergent, and pharmaceutical industries.53 Based on the mode of catalysis of peptide chain, there are endopeptidase like serine endopeptidase, cysteine peptidase, aspartic endopeptidases, metallopeptidases, and so on, and exopeptidases such as aminopeptidase, carboxypeptidase, and so on. The endopeptidase acts on the inner regions of peptide chain whereas the exopeptidases are sensitive to the terminal amino or carboxylic position of chain only.54 Proteases are beneficial for the manufacture of cheese, detergent, non-calorific artificial sweetener, and effective therapeutic agents. The alkaline proteases are useful for removing hairs in the leather industry. Subtilisin in combination with antibiotics is helpful in the treatment of burns and wounds.55
Factors Responsible for Spatial Distribution of in Soil
Published in Suhaib A. Bandh, Javid A. Parray, Nowsheen Shameem, Climate Change and Microbial Diversity, 2023
Protease enzyme is widely distributed in soils and shows a range of activities. It is involved in the hydrolysis of proteins into simple amino acids. Hydrolytic degradation of proteins by proteolytic enzymes is an important part of nitrogen cycle. Protease is present in all types of organisms ranging from microorganisms, plants, and animals. The steps of degradation of protein include conversion of protein into polypeptides to oligopeptides to finally amino acids with in nitrogen cycle (Mosier, 2001). The rate limiting step of nitrogen cycling is the protein hydrolysis and thus increasing the soil fertility. The production and activity of soil protease are controlled by various external factors which include climate, soil properties, and the substrate level from plants and microbial origin. Various researches are being conducted on the regulation of protease enzyme by using low molecular weight molecules or organic compounds like amino acids, phytohormones, siderophores, and flavonoids (Vranova et al., 2013). Based on the sites of cleavage in protein molecule which protease catalyzes, protease is categorized into two major groups. The first group called exopeptidase targets the terminal ends of protein and the second group called endopeptidase targets within the protein. Endopeptidase is classified into different forms according to their catalytic mechanisms, such as aspartic endopeptidase, cysteine endopeptidase, glutamic endopeptidase, metalloendopeptidase, serine endopeptidase, and threonine endopeptidase. Apart from these, protease also has an additional type, which is reserved for those which specifically act on peptides. These are termed as oligopeptidase (Britannica, 2020).
Mathematical modeling of enzymatic hydrolysis of soybean meal protein concentrate
Published in Chemical Engineering Communications, 2022
Cristine De Pretto, Liceres Correa de Miranda, Paula Fernandes de Siqueira, Marcelo Perencin de Arruda Ribeiro, Paulo Waldir Tardioli, Roberto de Campos Giordano, Raquel de Lima Camargo Giordano, Caliane Bastos Borba Costa
Wang et al. (2012) studied fitting both the Michaelis-Menten model and the exponential model, but only the latter described well the kinetics of soy protein isolate (SPI) by a trypsin-like endopeptidase. On the other hand, defatted wheat germ protein hydrolyzed by Alcalase in a continuous enzymatic hydrolysis reactor coupled to continuous removal of products by membrane separation was well described by the Michaelis-Menten model (Qu et al. 2013). The Michaelis-Menten with uncompetitive inhibition model was successfully adjusted to the experimental data of hydrolysis of corn gluten by Alcalase (Apar and Özbek 2010). As can be observed, different proteins, enzymes, and process conditions present different process behavior. Thus, it is not possible to generalize and predict in advance the behavior of a certain protein being hydrolyzed by a given enzyme. Therefore, a new assessment of the hydrolysis kinetic behavior is necessary when changing the protein, the enzyme, or the medium in which they are inserted.
Purification and characterization of fibrinolytic protease from Bacillus amyloliquefaciens MCC2606 and analysis of fibrin degradation product by MS/MS
Published in Preparative Biochemistry & Biotechnology, 2018
Yogesh Devaraj, Savita Kumari Rajender, Prakash Motiram Halami
The Bacillus sp. CFR15 was identified to be B. amyloliquefaciens. The CFR15-protease produced by this strain was found to possess both fibrinolytic and fibrinogenolytic activity. The CFR15-protease is of 32 kDa in size and is an alkaline protease, with optimum pH and temperature of 10.5 and 45°C, respectively. The inhibitors PMSF and EDTA had profound inhibitory activity and the metal ion Mn2+ slightly increased the activity of the enzyme. The degradation activity of the protease was more toward the fibrin than other protein substrates which is a desirable quality for any fibrinolytic enzyme. There is a need for thrombolytic agent which is more specific to fibrin than to other endogenous proteins. The CFR15-protease was found to be endopeptidase based on the degradation pattern of fibrin and fibrinogen. Analysis of initial fibrin degradation product confirmed higher susceptibility of β-chain for degradation among all other chains of fibrin. Detailed understanding of structural and functional properties of CFR15-protease may help in designing fibrin specific enzyme. The addition of enzyme food systems may help in developing functional foods for thrombosis related disorders. Further, N-terminal sequencing needs to be performed to future studies to understand the nature of enzyme.
Comparative functional and spectroscopic analysis of spent hen meat hydrolysate by individual and combined treatment of microbial proteases
Published in Preparative Biochemistry & Biotechnology, 2021
Deepak Kumar, Aakash Jyoti, Ayon Tarafdar, Aman Kumar, Prarabdh C. Badgujar
Stable free radical: 1,1-diphenyl-2-picrylhydrazyl (DPPH), 2,4,6-tripyidyltriazine (TPTZ), ferrozine, ferric chloride, ferrous sulfate, and salicylic acid were purchased from Sigma-Aldrich (Bengaluru India). Enzymes, Alcalase® 2.4 L (endopeptidase from Bacillus lichenformis) and Flavourzyme®500 L (endopeptidase and exopeptidase from Aspergillus oryzae) were purchased from Sigma-Aldrich (India). All other chemicals used were of analytical grade.