Enzymes for Research, Diagnostic and Industrial Use
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Catalog | Product Name | EC No. | CAS No. | Source | Price |
---|---|---|---|---|---|
NATE-0997 | Native Streptomyces griseus Pronase | EC 3.4.24.4 | 70851-98-8 | Streptomyces gr... | Inquiry |
Pronase is a mixture of protein hydrolases that have been at the forefront of a variety of scientific and industrial applications ranging from tissue dissociation to protein sequencing. Originally discovered in the late 1960's, pronase is a mixture of potent protein hydrolases derived from the extracellular filtrate of Streptomyces griseus. This complex mixture of enzymes consists primarily of serine proteases, metalloproteases, and other enzymes. The unique composition of pronase gives it the extraordinary ability to cleave peptide bonds, thereby breaking down proteins into smaller peptides and amino acids. This fundamental ability makes pronase an invaluable tool for a wide variety of scientific and industrial applications.
The structure of pronase proves its versatility. This enzyme complex consists of a variety of proteases, mainly serine proteases and metalloproteases. Among these enzymes, subtilisin, a serine protease, is the main component and is responsible for hydrolyzing peptide bonds. Together with the presence of other enzymes, this gives pronase a wide range of substrate specificity and the ability to efficiently degrade a wide variety of proteins. The intricate molecular structure of pronase has allowed it to exhibit unparalleled catalytic efficiency, making it an important tool in numerous enzymatic processes.
Protein kinases exert their catalytic effects through mechanisms of protein hydrolysis that are both broad and specific. Serine proteases, one of the major components of pronase, initiate the cleavage of peptide bonds via nucleophilic serine residues within their active sites. This mechanism enables pronase to hydrolyze proteins, thereby degrading large protein substrates into smaller peptides and amino acids. In addition, the presence of metalloproteinases further enhances the catalytic range of Pronase, allowing it to act on substrates that may not be efficiently cleaved by serine proteases alone. This dynamic and synergistic mechanism highlights the versatility and efficacy of pronase in protein degradation and modification.
Pronase is an indispensable tool for tissue dissociation and cell separation in scientific research. Its protein hydrolysis breaks down the extracellular matrix, facilitating the extraction of cells from tissues. This has proven critical in a variety of biological studies such as cell culture, stem cell research, and isolation of specific cell populations for downstream analysis.
Protein sequencing is a fundamental technique in biochemistry and molecular biology, and Pronase plays a pivotal role in protein sequencing. It cleaves proteins at specific peptide bonds and plays an important role in elucidating the sequence of amino acids in proteins. This is particularly important for understanding the structure and function of proteins and for identifying unknown or novel proteins.
In addition to scientific research, pronase is widely used in industrial processes. It is used in the pharmaceutical, food, and detergent industries. In the pharmaceutical field, pronase is used to produce protein hydrolysates for use as nutritional supplements. In addition, its role in the food industry includes tenderizing meat by breaking down tough protein fibers. In the detergent industry, pronase helps formulate enzymatic laundry detergents that effectively remove tough protein stains from fabrics.
The far-reaching impact of pronase spans a wide range of scientific and industrial fields, underscoring its significance as a transformative enzymatic tool. From scientific research to industrial processes, pronase's versatility stems from its complex structure and varied mechanisms, which have propelled it to the forefront of countless applications, providing versatile enzymatic solutions to a wide range of challenges.