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Proteolytic enzymes

About: Proteolytic enzymes is a research topic. Over the lifetime, 23096 publications have been published within this topic receiving 835544 citations.


Papers
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Journal ArticleDOI
TL;DR: In this review, identified bioactivities and potentialities of marine algal protein sources will be discussed for future pharmaceutical, nutraceutical and cosmeceutical applications.

229 citations

Journal ArticleDOI
TL;DR: This Review summarizes the fascinating roles of ADAMs in embryonic and adult tissue development in both vertebrates and invertebrates.
Abstract: Proteolytic enzymes belonging to the A Disintegin And Metalloproteinase (ADAM) family are able to cleave transmembrane proteins close to the cell surface, in a process referred to as ectodomain shedding. Substrates for ADAMs include growth factors, cytokines, chemokines and adhesion molecules, and, as such, many ADAM proteins play crucial roles in cell-cell adhesion, extracellular and intracellular signaling, cell differentiation and cell proliferation. In this Review, we summarize the fascinating roles of ADAMs in embryonic and adult tissue development in both vertebrates and invertebrates.

229 citations

Journal ArticleDOI
TL;DR: In this paper, the peptides have been identified within the amino acid sequences of native milk proteins and their full activities are manifested upon proteolytic digestion to release and activate encrypted bioactive peptides from the original protein.
Abstract: Functionally and physiologically active peptides are produced from several food proteins during gastrointestinal digestion and fermentation of food materials with lactic acid bacteria. Once bioactive peptides (BPs) are liberated, they exhibit a wide variety of physiological functions in the human body such as gastrointestinal, cardiovascular, immune, endocrine, and nervous systems. These functionalities of the peptides in human health and physiology include antihypertensive, antimicrobial, antioxidative, antithrombotic, opioid, anti-appetizing, immunomodulatory and mineral-binding activities. Most of the bioactivities of milk proteins are latent, being absent or incomplete in the original native protein, but full activities are manifested upon proteolytic digestion to release and activate encrypted bioactive peptides from the original protein. Bioactive peptides have been identified within the amino acid sequences of native milk proteins. Due to their physiological and physico-chemical versatility, milk peptides are regarded as greatly important components for health promoting foods or pharmaceutical applications. Milk and colostrum of bovine and other dairy species are considered as the most important source of natural bioactive components. Over the past a few decades, major advances and developments have been achieved on the science, technology and commercial applications of bioactive components which are present naturally in the milk. Although the majority of published works are associated with the search of bioactive peptides in bovine milk samples, some of them are involved in the investigation of ovine or caprine milk. The advent of functional foods has been facilitated by increasing scientific knowledge about the metabolic and genomic effects of diet and specific dietary components on human health.

229 citations

Journal ArticleDOI
TL;DR: A considerable part of the authors' current knowledge about mechanism and biochemistry of lysosomal lipid degradation is derived from a class of human diseases, the sphingolipidoses, which are caused by inherited defects within sphingoipid and glycosaminoglycans catabolism.

229 citations

Book ChapterDOI
TL;DR: Staphylococcal protease can be used for the determination of the amino acid sequences of several proteins and proved to be another valuable tool for such studies.
Abstract: Publisher Summary Proteolytic enzymes catalyzing the hydrolysis of peptide bonds involving exclusively the basic amino acid residues lysine and arginine have been available for many years. Trypsin is by far the best known enzyme exhibiting this high degree of specificity and, for that reason, it has played a central role in the studies of the primary structure of proteins. Recently, enzymes that specifically cleave peptide bonds at the carboxyl group of the acidic amino acid residues, aspartic acid and glutamic acid, have been discovered. One of these enzymes, staphylococcal protease, has this specificity and can be further restricted to glutamyl bonds only under certain controlled conditions. This enzyme can be used for the determination of the amino acid sequences of several proteins and proved to be another valuable tool for such studies. Staphylococcal protease shows a marked preference for certain aspartyl bonds when used in ammonium bicarbonate or acetate buffer. The staphylococcal protease is fully active in the presence of 0.2% sodium dodecyl sulfate and retains 50% of its activity in a 4 M urea solution. Digestion under these conditions could be attempted for proteins or peptides that are not readily attacked by the protease under nondenaturing conditions.

228 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202350
2022113
2021358
2020434
2019358
2018472