PEPTIDASES

Peptidases are also involved in various cellular processes, such as the regulation of protein activity, cell cycle progression, and apoptosis (programmed cell death).
Peptidases are classified into different types based on their catalytic mechanisms.
Peptidases produced by submerged fermentation of a selected strain of Bacillus amyloliquefaciens.

CAS Number: 37259-58-8
EC Number: 253-431-3

Synonyms: Serine proteinase, 37259-58-8, Serine endopeptidase, Serine esterase, Serine peptidase, Serine protease, Seryl protease, Tryase, Proteinase, serine, Caldolase, Cerastobin, Clp proteinase, EINECS 253-431-3, alpha-Fibrinogenase, Maxacal, Porzyme 6, Proteinase T, Serine Proteases

Peptidases can be found in all forms of life and viruses.
They have independently evolved multiple times, and different classes of Peptidases can perform the same reaction by completely different catalytic mechanisms.

Peptidases were first grouped into 84 families according to their evolutionary relationship in 1993, and classified under four catalytic types: serine, cysteine, aspartic, and metalloPeptidases.
A Peptidases is an enzyme that catalyzes the hydrolysis of peptide bonds in proteins.

These enzymes play a crucial role in the digestion of proteins in organisms, breaking them down into smaller peptides or individual amino acids.
The major classes include serine Peptidases, cysteine Peptidases, aspartic Peptidases, metalloPeptidases, and threonine Peptidases.

Each class of Peptidases has distinct properties and is involved in specific biological processes.
Secretion of Peptidases by Bacillus amyloliquefaciens can be inhibited by treatment with the fatty acid synthetase inhibitor cerulenin.

A Peptidases (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products.
They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds.

Peptidases are involved in numerous biological pathways, including digestion of ingested proteins, protein catabolism (breakdown of old proteins), and cell signaling.
In the absence of functional accelerants, proteolysis would be very slow, taking hundreds of years.

The threonine and glutamic Peptidases were not described until 1995 and 2004 respectively.
The mechanism used to cleave a peptide bond involves making an amino acid residue that has the cysteine and threonine (Peptidases) or a water molecule (aspartic, glutamic and metalloPeptidases) nucleophilic so that Peptidases can attack the peptide carbonyl group.

One way to make a nucleophile is by a catalytic triad, where a histidine residue is used to activate serine, cysteine, or threonine as a nucleophile.
This is not an evolutionary grouping, however, as the nucleophile types have evolved convergently in different superfamilies, and some superfamilies show divergent evolution to multiple different nucleophiles.

MetalloPeptidases, aspartic, and glutamic Peptidases utilize their active site residues to activate a water molecule, which then attacks the scissile bond.
Peptidases can be highly promiscuous such that a wide range of protein substrates are hydrolyzed.

This is the case for digestive enzymes such as trypsin, which have to be able to cleave the array of proteins ingested into smaller peptide fragments.
Promiscuous Peptidases typically bind to a single amino acid on the substrate and so only have specificity for that residue.
For example, trypsin is specific for the sequences.

Conversely some Peptidases are highly specific and only cleave substrates with a certain sequence.
Blood clotting (such as thrombin) and viral polyprotein processing (such as TEV Peptidases) requires this level of specificity in order to achieve precise cleavage events.

Peptidases are enzymes that break down protein.
These enzymes are made by animals, plants, fungi, and bacteria.

Peptidases break down proteins in the body or on the skin.
This might help with digestion or with the breakdown of proteins involved in swelling and pain.

Some Peptidases that may be found in supplements include bromelain, chymotrypsin, ficin, papain, serrapeptase, and trypsin.
Peptidases, as also called Protease or proteinases, are enzymes that perform proteolysis.

Peptidases is one of the most important biological reactions.
Peptidases activity has been attributed to a class of enzymes called Peptidases.

These enzymes are of wide distribution, and they perform significant biological processes.
Peptidases have evolved to perform these reactions by numerous different mechanisms and different classes of Peptidases can perform the same reaction by completely different catalytic mechanisms.

Peptidases are found in animals, plants, bacteria, archaea, and viruses.
Peptidases are involved in protein processing, regulation of protein function, apoptosis, viral pathogenesis, digestion, photosynthesis, and numerous other vital processes.

Peptidases mechanism of action classifies them as either serine, cysteine or threonine Peptidases (amino-terminal nucleophile hydrolases), or as aspartic, metallo and glutamic Peptidases (with glutamic Peptidases being the only subtype not found in mammals so far).
Peptidases of peptide bonds is recognized as an essential and ubiquitous mechanism for the regulation of a myriad of physiological processes.

Four main classes of proteolytic enzymes have been routinely utilized to describe Peptidases.
The serine Peptidases are probably the best characterized.

This class of Peptidases includes trypsin, chymotrypsin and elastase.
The cysteine Peptidases class includes papain, calpain and lysosomal cathepsins.

Aspartic Peptidases include pepsin and rennin.
Metallo-Peptidases include thermolysin and carboxypeptidase A.

Peptidases are enzymes that cleave peptide bonds in proteins.
Peptidases serves as the nucleophilic amino acid at the (enzyme's) active site.

They are found ubiquitously in both eukaryotes and prokaryotes.
Peptidases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like.

Peptidases is a general term for a class of enzymes that hydrolyze protein peptide bonds.
According to the manner in which the polypeptide is hydrolyzed, Peptidases can be divided into two types, an endopeptidase and an exopeptidase.

The endopeptidase cleaves the inside of the protein molecule to form a small molecular peptide.
The exopeptidase hydrolyzes the peptide bond one by one from the terminal of the free amino group or carboxyl group of the protein molecule, and the amino acid is released, the former being an aminopeptidase and the latter being a carboxypeptidase.

Peptidases can be further divided into serine Peptidases, thiol Peptidases, metallo proteinase and aspartic Peptidases according to its active center.
According to the optimum pH value of the reaction, Peptidases is divided into acid Peptidases, neutral Peptidases and alkaline Peptidases.

Peptidases is used in industrial production, mainly endopeptidase.
Peptidases are widely found in animal viscera, plant stems, leaves, fruits and microorganisms. Microbial Peptidases are mainly produced by molds and bacteria, followed by yeasts and actinomycetes.

Peptidases have many types, and important ones are pepsin, trypsin, cathepsin, papain, and subtilisin.
Peptidases has strict selectivity for the reaction substrate to be applied.

Peptidases can only act on certain peptide bonds in the protein molecules, such as peptide bonds formed by trypsin catalyzed hydrolysis of basic amino acids.
Peptidases is a widely distributed protein, and is especially abundant in the digestive tract of humans and animals.

Due to the limited resources of animals and plants, the industrial production of Peptidases preparations is mainly prepared by fermentation of microorganisms such as Bacillus subtilis and Aspergillus oryzae.
Peptidases are a class of proteins that break down other proteins.

They are also called proteolytic enzymes.
Peptidases are classified by the amino acids or ligands that catalyze the hydrolysis reaction.
For example, Peptidases contain a serine in the active site.

The Peptidases is helped by a neighboring histidine and aspartic acid.
This combination is called the catalytic triad, and is conserved in all serine Peptidases.

Peptidases work in a two step fashion; first, they form a covalent bond with the protein to be cleaved; in the second step, water comes in and releases the second half of the cleaved protein.
Peptidases use cysteine as a nucleophile just like serine Peptidases use serine as a nucleophile.
Peptidases include a number of digestive enzymes, including Trypsin, Chymotrypsin, and Elastase.

While they all contain the same three amino acids that work together to catalyze the reaction, called the catalytic triad, they differ in where they cleave proteins.
This specificity is due to a binding pocket that contains different functional groups.

Chymotrypsin prefers a large hydrophobic residue; Peptidases pocket is large and contains hydrophobic residues.
In this representation of the binding pocket, the hydrophobic phenylalanine of the substrate is shown in green, and the hydrophobicity of the surrounding amino acids is shown by grey (hydrophobic) or purple (hydrophilic) balls.

Peptidases is specific for positively charged residues like lysine, and contains a negative amino acid, aspartic acid, at the bottom of the pocket.
Peptidases prefers a small neutral residue; Peptidases has a very small pocket.

Peptidases include enzymes that have a role in regulating cellular processes such as caspases and deubiquitinase.
Caspases hydrolyze proteins during apoptosis.
Peptidases play a role in regulating protein degradation, e.g. Cdu1 from Chlamydia.

Another class of Peptidases is aspartate Peptidases.
This family includes HIV Peptidases.

HIV produces Peptidases proteins as one long chain; HIV Peptidases cleaves the long protein into functional units.
Because Peptidases cleaves long proteins, Peptidases has a tunnel to accommodate the long peptide substrate, and the top "flaps" of the protein can open and closeto allow the substrate in and products out.

Aspartate Peptidases include two aspartate residues in the active site, which increase the reactivity of an active site water molecule to directly cleave the substrate protein.
A third class of Peptidases are metalloPeptidases such as carboxypeptidase.

CarboxyProtease remove the C terminal amino acids from proteins.
The active site contains zinc , which is bound to the protein through interactions with histidine (H), serine (S) aspartic acid (E) residues.

Proteolytic enzymes (Peptidases) are enzymes your pancreas makes to break down protein from diet into amino acids, which are used for growth and tissue repair.
These enzymes may also reduce inflammation and support immune function, though more research is needed.

Peptidases (also called Proteolytic Enzymes, Protease, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides.
Most Peptidases act in a specific manner, hydrolyzing bonds at or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide.

Peptidases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer.
They are also an important research tool, frequently used in the analysis and production of proteins.

Peptidases have been called biology’s version of Swiss army knives, able to cut long sequences of proteins into fragments.
A Peptidases is an enzyme that breaks the long, chainlike molecules of proteins so they can be digested.

This process is called proteolysis, and Peptidases turns protein molecules into shorter fragments, called peptides, and eventually into their components, called amino acids.
Proteins start as a tough, complex, folded structure, and they can only be broken down or disassembled with Peptidases enzymes.

The process of digesting proteins starts in the stomach, where hydrochloric acid unfolds the proteins and the enzyme pepsin begins to disassemble them.
The pancreas releases Peptidases enzymes (primarily trypsin), and in the intestines, they break protein chains apart into smaller pieces.
Then enzymes on the surface and inside of intestinal cells break the pieces down even further, so they become amino acids that are ready for use throughout the body.

When these Peptidases enzymes aren’t present in the body to break down protein molecules, the intestinal lining would not be able to digest them, which can lead to some serious health issues.
Peptidases are produced by the pancreas, and they are also found in some fruits, bacteria and other microbes.

The digestive tract produces three different forms of Peptidases in digestive tracts: trypsinogen, chymotrypsinogen and procarboxypeptidase.
These three Peptidases attack different peptide linkages to allow for the generation of amino acids, the building blocks of protein.

Peptidases enzymes are often classified based on their origins.
Some Peptidases are produced in bodies, some come from plants and others have a microbial origin.

Different types of Peptidases have different biological processes and mechanisms.
Peptidases are enzymes that specialize in the cleavage of peptide bonds.

Their activities may be relatively indiscriminate, breaking polypeptides down to their basic elements, or exquisitely precise, cleaving a substrate at a specific residue to alter protein activity.
These illustrations highlight scientific concepts that rely on proteolytic activity and emphasize the importance of Peptidases in some of the most studied areas of cell biology.

These enzymes contain a serine residue in their active site and play crucial roles in digestion (e.g., trypsin, chymotrypsin) and blood clotting (e.g., thrombin).
Enzymes with a cysteine residue in their active site, involved in various cellular processes, including apoptosis. Examples include caspases.

These enzymes use an aspartate residue in their active site and are involved in digestion (e.g., pepsin) and some viral processing.
Metal ions, typically zinc, are essential for the catalytic activity of these enzymes.
Matrix metalloproteinases (MMPs) are an example, involved in tissue remodeling and wound healing.

These Peptidases have a threonine residue in their active site and are found in certain microorganisms.
In the digestive system, Peptidases break down dietary proteins into smaller peptides and amino acids, facilitating their absorption in the small intestine.

Peptidases are involved in regulating various cellular processes, including cell cycle progression, apoptosis, and signal transduction.
Some Peptidases are responsible for activating or inactivating proteins by cleaving specific peptide bonds.

Peptidases participate in immune responses by degrading foreign proteins, such as those from pathogens.
Peptidases are used in laundry detergents and cleaning products to break down protein-based stains.

Peptidases can be employed to cleave specific peptide tags used in recombinant protein production, aiding in the purification of the target protein.
Peptidases inhibitors and activators are used in drug development for various medical conditions, including HIV, cancer, and neurodegenerative diseases.

Peptidases are essential tools in molecular biology for protein analysis, structure-function studies, and manipulation of proteins.
Peptidases are a class of enzymes that catalyze the hydrolysis of peptide bonds in proteins, is one of the most mature.

At the beginning of the 21st century, microbial Peptidases has been reported more than 900 species, the biological activities of the organism and the occurrence of diseases, such as digestion and absorption of food, blood coagulation, hemolysis, inflammation, blood pressure regulation, cell differentiation autolysis, aging, cancer metastasis, activation of physiologically active peptides, etc., are not related to Peptidases.

Peptidases are closely related to humans and are involved in all aspects of life.
Peptidases are widely used in food, pharmaceutical, chemical, detergent, feed and other fields, the gross product reached 65% of the enzyme market.

Peptidases is a kind of enzyme that catalyzes the hydrolysis of protein, which is the earliest and the most in-depth enzyme in the study of Enzymology.
Microbial Peptidases source is wide, Cell Nutrition requirement is low, easy to culture, compared with animal and plant source Peptidases, Peptidases is easier to realize large-scale production.

Early research on microbial Peptidases, more concentrated in the breeding of natural high-yield strains, optimization of fermentation conditions and downstream processing technology, the overall research level is not high, did not really take into account, various aspects of large-scale production technology.
Until the 70 s of the 20th century, after the establishment of recombinant DNA technology, the research in the field of Peptidases molecular biology was carried out, and the sequence analysis, cloning and expression of Peptidases genes were realized, which made the large-scale production possible.

A seventh catalytic type of proteolytic enzymes, asparagine peptide lyase, was described in 2011.
Peptidases proteolytic mechanism is unusual since, rather than hydrolysis, Peptidases performs an elimination reaction.
During this reaction, the catalytic asparagine forms a cyclic chemical structure that cleaves itself at asparagine residues in proteins under the right conditions.

Given Peptidases fundamentally different mechanism, its inclusion as a peptidase may be debatable.
An up-to-date classification of Peptidases evolutionary superfamilies is found in the MEROPS database.
In this database, Peptidases are classified firstly by 'clan' (superfamily) based on structure, mechanism and catalytic residue order (e.g. the PA clan where P indicates a mixture of nucleophile families).

Within each 'clan', Peptidases are classified into families based on sequence similarity (e.g. the S1 and C3 families within the PA clan).
Each family may contain many hundreds of related Peptidases (e.g. trypsin, elastase, thrombin and streptogrisin within the S1 family).

Peptidases, being themselves proteins, are cleaved by other Peptidases molecules, sometimes of the same variety.
This acts as a method of regulation of Peptidases activity.

Some Peptidases are less active after autolysis (e.g. TEV Peptidases) whilst others are more active (e.g. trypsinogen).
In the human digestive system, Peptidases like pepsin, trypsin, and chymotrypsin break down dietary proteins into smaller peptides and amino acids, facilitating their absorption in the small intestine.

Peptidases are commonly used in laundry detergents and cleaning products for their ability to break down protein-based stains.
This is particularly effective in removing stains like blood, grass, and food.

Peptidases can be used to tenderize meat by breaking down collagen and connective tissues.
Peptidases contribute to the development of flavors in certain food products by breaking down proteins into smaller, more palatable fragments.

Dairy Processing: Peptidases are used in cheese production to modify texture and flavor.
Peptidases play a crucial role in protein purification.

They are used to cleave fusion tags from recombinant proteins, facilitating their isolation and purification.
Peptidases inhibitors are important in drug development, especially in the treatment of diseases where Peptidases activity needs to be modulated.
For example, Peptidases inhibitors are used in the treatment of HIV.

Researchers modify and engineer Peptidases for specific applications.
This may involve altering their substrate specificity, stability, or other properties to suit industrial or therapeutic purposes.

Peptidases are valuable tools in molecular biology and biochemistry research.
Techniques such as limited proteolysis are used to study protein structure, function, and interactions.

Certain Peptidases, such as matrix metalloproteinases (MMPs), play a role in tissue remodeling.
Understanding and controlling Peptidases activity is important in applications related to wound healing and tissue engineering.

Some Peptidases are used as diagnostic tools.
For example, the prostate-specific antigen (PSA) is a Peptidases used as a biomarker for prostate cancer.

Peptidases are used in bioremediation processes to degrade proteins present in organic waste.
This can be useful in environmental cleanup efforts.

Peptidases are sometimes used in cosmetics for exfoliation purposes.
They can help remove dead skin cells and improve skin texture.

Peptidases occur in all organisms, from prokaryotes to eukaryotes to virus.
These enzymes are involved in a multitude of physiological reactions from simple digestion of food proteins to highly regulated cascades (e.g., the blood-clotting cascade, the complement system, apoptosis pathways, and the invertebrate prophenoloxidase-activating cascade).

Peptidases can either break specific peptide bonds (limited proteolysis), depending on the amino acid sequence of a protein, or completely break down a peptide to amino acids (unlimited proteolysis).
The activity can be a destructive change (abolishing a protein's function or digesting Peptidases to its principal components), Peptidases can be an activation of a function, or Peptidases can be a signal in a signalling pathway.

Peptidases are used throughout an organism for various metabolic processes.
Acid Peptidases secreted into the stomach (such as pepsin) and serine Peptidases present in the duodenum (trypsin and chymotrypsin) enable us to digest the protein in food.

Peptidases present in blood serum (thrombin, plasmin, Hageman factor, etc.) play an important role in blood-clotting, as well as lysis of the clots, and the correct action of the immune system.
Other Peptidases are present in leukocytes (elastase, cathepsin G) and play several different roles in metabolic control.

Some snake venoms are also Peptidases, such as pit viper haemotoxin and interfere with the victim's blood clotting cascade.
Peptidases determine the lifetime of other proteins playing important physiological roles like hormones, antibodies, or other enzymes.

This is one of the fastest "switching on" and "switching off" regulatory mechanisms in the physiology of an organism.
Bacteria secrete Peptidases to hydrolyse the peptide bonds in proteins and therefore break the proteins down into their constituent amino acids.

Bacterial and fungal Peptidases are particularly important to the global carbon and nitrogen cycles in the recycling of proteins, and such activity tends to be regulated by nutritional signals in these organisms.
The net impact of nutritional regulation of Peptidases activity among the thousands of species present in soil can be observed at the overall microbial community level as proteins are broken down in response to carbon, nitrogen, or sulfur limitation.

The genomes of some viruses encode one massive polyprotein, which needs a Peptidases to cleave this into functional units (e.g. the hepatitis C virus and the picornaviruses).
These Peptidases (e.g. TEV Peptidases) have high specificity and only cleave a very restricted set of substrate sequences.

They are therefore a common target for Peptidases inhibitors.
Cells often produce Peptidases inhibitors to regulate the activity of Peptidases.

These inhibitors bind to Peptidases and prevent them from catalyzing the hydrolysis of peptide bonds.
This regulation is crucial for maintaining a balance in cellular processes.

Altered activity of Peptidases is associated with cancer progression.
Matrix metalloproteinases (MMPs), for example, are implicated in tumor invasion and metastasis.

Peptidases, such as proteasomes, are involved in the clearance of misfolded proteins.
Dysregulation of Peptidases has been linked to neurodegenerative disorders like Alzheimer's and Parkinson's disease.

Proteasomes are large protein complexes responsible for degrading unneeded or damaged proteins in the cell.
They play a crucial role in maintaining cellular homeostasis by regulating the concentration of specific proteins.

In the context of HIV (human immunodeficiency virus) infection, Peptidases inhibitors are a class of antiretroviral drugs.
They block the activity of the HIV Peptidases enzyme, preventing the virus from producing infectious particles.

Scientists engage in Peptidases engineering to modify and optimize Peptidases for specific applications.
This involves altering their substrate specificity, stability, or other properties for industrial or therapeutic purposes.

Researchers use Peptidases as tools in the lab to study protein structure and function.
Techniques like limited proteolysis involve treating proteins with Peptidases to identify structural domains or determine conformational changes.

Peptidases are employed in the food industry for various purposes.
For example, they can be used in the production of certain foods to enhance flavor or texture.

Additionally, Peptidases play a role in the tenderization of meat.
Caspases, a family of cysteine Peptidases, play a central role in the process of apoptosis.

They cleave specific proteins, leading to the controlled dismantling of the cell.
Peptidases are targets for drug discovery.

Developing drugs that specifically inhibit or activate certain Peptidases can have therapeutic implications, especially in conditions where Peptidases dysregulation is involved.
The activity of Peptidases is inhibited by Peptidases inhibitors.

One example of Peptidases inhibitors is the serpin superfamily.
Peptidases includes alpha 1-antitrypsin (which protects the body from excessive effects of Peptidases own inflammatory Peptidases), alpha 1-antichymotrypsin (which does likewise), C1-inhibitor (which protects the body from excessive Peptidases-triggered activation of Peptidases own complement system), antithrombin (which protects the body from excessive coagulation), plasminogen activator inhibitor-1 (which protects the body from inadequate coagulation by blocking Peptidases-triggered fibrinolysis), and neuroserpin.

Natural Peptidases inhibitors include the family of lipocalin proteins, which play a role in cell regulation and differentiation.
Lipophilic ligands, attached to lipocalin proteins, have been found to possess tumor Peptidases inhibiting properties.

The natural Peptidases inhibitors are not to be confused with the Peptidases inhibitors used in antiretroviral therapy.
Some viruses, with HIV/AIDS among them, depend on Peptidases in their reproductive cycle.

Thus, Peptidases inhibitors are developed as antiviral therapeutic agents.
Other natural Peptidases inhibitors are used as defense mechanisms.

Common examples are the trypsin inhibitors found in the seeds of some plants, most notable for humans being soybeans, a major food crop, where they act to discourage predators.
Raw soybeans are toxic to many animals, including humans, until the Peptidases inhibitors they contain have been denatured.

Proteolytic enzymes are essential for many important processes in your body.
They’re also called Protease or proteinases.

In the human body, they are produced by the pancreas and stomach.
While proteolytic enzymes are most commonly known for their role in the digestion of dietary protein, they perform many other critical jobs as well.
For example, they are essential for cell division, blood clotting, immune function and protein recycling, among other vital processes (1Trusted Source).

Like humans, plants also depend on proteolytic enzymes throughout their life cycles.
Not only are these enzymes necessary for the proper growth and development of plants, they also help keep them healthy by acting as a defense mechanism against pests like insects.

Interestingly, people can benefit from ingesting plant-derived proteolytic enzymes.
As a result, proteolytic enzyme supplements may contain both animal- and plant-derived enzymes.
Peptidases (both endo- and exo- types with no systemic name) are enzymes that are commercially derived from the fungus, Aspergillus oryzae or Aspergillus niger, via a fermentation process.

During the recovery phase of production, manufacturers destroy the starting fungi, A. oryzae or A. niger, before removing the non-proteinaceous material away from the Peptidases preparation.
Peptidases are recovered from the fermentation broth in an aqueous solution and then processed to a dried state.

Uses of Peptidases:
Peptidases from Bacillus amyloliquefaciens has been used for the unhairing of hides and skins.
Peptidases has also been used in a study to investigate peptide bond formation using the carbamoylmethyl ester as the acyl donor.
The field of Peptidases research is enormous.

Since 2004, approximately 8000 papers related to this field were published each year.
Peptidases are used in industry, medicine and as a basic biological research tool.

Peptidases can be used to disrupt biofilms, which are communities of microorganisms encased in a protective matrix.
Breaking down the biofilm matrix helps in combating bacterial infections.

Researchers are exploring the use of Peptidases for targeted cancer therapies.
Peptidases can be designed to selectively activate prodrugs in cancer cells, minimizing damage to healthy tissues.

Peptidases inhibitors are being investigated for use in agriculture to protect crops from pests.
These inhibitors interfere with the digestive processes of certain insects, offering a potential eco-friendly pest control strategy.

Peptidases are used in skincare products for their exfoliating properties.
They help remove dead skin cells, promoting skin renewal and potentially reducing the appearance of fine lines and wrinkles.

Peptidases are incorporated into biosensors for detecting specific biomolecules.
The changes in fluorescence or other properties resulting from Peptidases activity can be used as signals for the presence of certain substances.

Peptidases are employed in biocatalytic processes for organic synthesis.
They can catalyze specific reactions with high selectivity, providing environmentally friendly alternatives to traditional chemical methods.

Certain Peptidases are explored as biopesticides to control insect pests in agriculture.
These Peptidases can disrupt insect digestive processes, leading to reduced feeding and growth.

Peptidases associated with tumor development and progression can be targeted for imaging purposes.
Peptidases-activated imaging agents can provide insights into the presence and activity of Peptidases in cancerous tissues.

Peptidases and their substrates are investigated as potential biomarkers for various diseases.
Detection of specific Peptidases activity patterns may aid in early disease diagnosis.

Understanding individual variations in Peptidases activity may contribute to the development of personalized medicine.
Tailoring treatments based on Peptidases profiles could enhance therapeutic efficacy.

Peptidases are being explored for environmental monitoring, particularly in assessing water quality.
Changes in Peptidases activity can indicate contamination or changes in microbial communities.

Digestive Peptidases are part of many laundry detergents and are also used extensively in the bread industry in bread improver.
A variety of Peptidases are used medically both for their native function (e.g. controlling blood clotting) or for completely artificial functions (e.g. for the targeted degradation of pathogenic proteins).

Highly specific Peptidases such as TEV Peptidases and thrombin are commonly used to cleave fusion proteins and affinity tags in a controlled fashion.
Peptidases-containing plant-solutions called vegetarian rennet have been in use for hundreds of years in Europe and the Middle East for making kosher and halal Cheeses.

Vegetarian rennet from Withania coagulans has been in use for thousands of years as a Ayurvedic remedy for digestion and diabetes in the Indian subcontinent.
Peptidases is also used to make Paneer.

Peptidases are utilized in the textile industry for processes such as desizing and finishing.
They help remove unwanted fibers and improve the texture and appearance of fabrics.

Peptidases can be employed in the production of biofuels.
They assist in the breakdown of plant cell walls, releasing sugars that can be fermented into biofuels.

Peptidases are used in the leather industry to aid in the dehairing and softening of hides during leather processing.
Peptidases can be used in the food industry to modify the properties of certain foods, such as enhancing the solubility of proteins in beverages or improving the texture of baked goods.

Some Peptidases, like thrombin, are used in medicine as anti-clotting agents.
They are employed in anticoagulant therapies to prevent abnormal blood clot formation.

Peptidases are used to hydrolyze proteins into smaller peptides and amino acids, contributing to the development of savory flavors in processed foods.
Peptidases can be applied in the pulp and paper industry to modify the characteristics of paper pulp, leading to improved paper quality.

Inflammatory diseases, such as rheumatoid arthritis, involve excessive Peptidases activity.
Therapies aimed at modulating Peptidases activity are being explored for potential treatment options.

Peptidases are used in fish feed formulations to improve the digestibility of proteins, promoting better growth and health in farmed fish.
Peptidases are being investigated for their potential use in decontaminating surfaces exposed to biological warfare agents.

They can break down proteins in these agents, rendering them harmless.
Peptidases are employed in various biochemical assays and tests to study enzyme kinetics, substrate specificity, and other aspects of enzymatic reactions.

Peptidases are commonly used in laundry detergents and stain removers.
They help break down protein-based stains, such as blood, grass, and food, making them easier to wash away.

Meat Tenderization: Peptidases are used to tenderize meat by breaking down collagen and connective tissues, improving the texture of the meat.
Peptidases are employed in cheese production to modify texture and flavor.

In brewing, Peptidases can be used to break down proteins that might cause haze in beer. In baking, they can improve the texture of dough.
Peptidases are used in biotechnology for protein purification.
They can be employed to cleave fusion tags from recombinant proteins, facilitating the isolation and purification of the desired protein.

Peptidases inhibitors are essential in drug development.
For example, Peptidases inhibitors are used in the treatment of HIV by inhibiting the viral Peptidases, preventing the maturation of new virus particles.
Peptidases may be used in enzyme replacement therapies for individuals with certain genetic disorders that result in deficient Peptidases activity.

Peptidases are valuable tools in molecular biology research.
Techniques such as limited proteolysis are used to study protein structure, function, and interactions.

Peptidases, such as matrix metalloproteinases (MMPs), play a role in tissue remodeling.
Understanding and controlling Peptidases activity is important in applications related to wound healing and tissue engineering.

Some Peptidases, like the prostate-specific antigen (PSA), are used as diagnostic biomarkers for certain medical conditions, such as prostate cancer.
Peptidases are used in bioremediation processes to degrade proteins present in organic waste, contributing to environmental cleanup efforts.

Peptidases are sometimes used in cosmetics for exfoliation purposes.
They can help remove dead skin cells and improve skin texture.
In certain medical conditions, enzyme replacement therapy involving Peptidases may be used to supplement deficient or missing enzyme activity in the body.

Classification of Peptidases:
Peptidases are divided into two categories: exoPeptidase and endopeptidases.
ExoPeptidase only act on the C- terminal or N-terminal peptide bonds of the substrate, endopeptidase can only hydrolyze the peptide bonds inside the macromolecular protein and is a true Peptidases.

There have been a variety of methods of classification of Peptidases, but they are not perfect, some to the active center, or to the mode of action, but also to the optimal pH value, academic to the active center to point.

Peptidases can be divided into four classes according to the active center:
(1) serine Peptidases
(2) aspartic Peptidases
(3) cysteine Peptidases
(4) metalloPeptidases.

Serine Peptidases enzymes are widely found in animal pancreas, bacteria, mold, the active center contains serine residues, enzyme activity can be, diisopropylphosphoryl fluoride (DFP), benzene methyl sulfonyl fluoride (PMSF) and potato inhibitors (PI) and other specific inhibition.
The optimum pH of the enzyme is alkaline Peptidases at 9.5~10.5, but some serine Peptidases are neutral Peptidases, and some enzymes also contain cysteine residues due to the active center, Peptidases can be inhibited by the thiol reagent to the chlorine Mercury benzoic acid (PCMB).

The specificity for the substrate is similar to that for chyme trypsin.
Metalloproteinases this kind of Peptidases is mainly neutral Peptidases, the optimum pH is 7~8, most of the active center contains Zn2 and other divalent metals, can be subject to metal chelating agent EDTA or phenanthroline (O-Phenanthroline,OP) the inhibition of such Peptidases is less stable, limited use, and less important than alkaline and acid Peptidases.

Metalloproteinases also include the alkaline Peptidases of Pseudomonas aeruginosa, snake venom and collagenase.
Microbial Metallo-neutral Peptidases, such as bacterial and fungal neutral Peptidases, can cleave amino-terminal peptide bonds composed of hydrophobic or other amino acid residues.
Aspartic acid Peptidases pepsin, fungal acid Peptidases is the active center containing aspartic acid acid Peptidases, the optimum pH of this kind of enzyme is 2.0~5.0, in acidic stability, rapid inactivation of the enzyme at pH above 6, PI 3-4.5, diazoacetyl-N-leucine methyl ester (DAN) and 1, 2-epoxy-3-(p-nitrophenyl) propane (EPNP), is an obligate inhibitor of this kind of enzyme, the molecular weight of the enzyme 30~45 kDa.

Cysteine Peptidases this kind of enzyme is also called thiol Peptidases, known that this kind of enzyme has about 20 families, widely exists in prokaryotes and eukaryotes, Peptidases active center contains a pair of amino acids that is Cys-His, different groups of enzymes before and after Cys and His in different order.
Typically, such enzymes require the presence of a reducing agent, such as HCN or cysteine, to be active.

Specificity of Peptidases:
The specificity of the Peptidases is expressed in the selectivity of the substrate peptide bond, Peptidases is not only affected by amino acid residues on one or both sides of the peptide bond at the cleavage point, but also sometimes affected by several amino acid residue units separated from the point of action, and also affected by the length of the peptide bond.
The study of the specificity of Peptidases is usually carried out with synthetic substrates of known sequence, for the above reasons, often inconsistent with the hydrolysis of natural proteins.

Production of Peptidases:
Peptidases is widely used, which not only simplifies the production process of relevant industries, but also saves investment, Peptidases reduces the consumption of raw materials, improves the yield and quality of products, and makes a positive contribution to improving environmental protection and reducing carbon dioxide emissions.
The factors affecting the production of microbial Peptidases is very complex, the same microorganism because of different culture conditions, can produce a variety of Peptidases, most of the bacillus is aerobic non-toxin and non-pathogenic, easy to culture.
Microbial Peptidases enzyme composition is very complex, the same enzyme electrophoresis, chromatography and other separation techniques, but also can separate a number of molecular weight, amino acid composition, optimum pH, temperature and isoelectric point of different composition, the similarities and differences in the amino acid sequence and conformation of the enzyme can also be seen by the immunological antigen antibody reaction.

Safety Profile of Peptidases:
Peptidases can be irritating to the skin and eyes, particularly at higher concentrations.
Direct contact with Peptidases-containing solutions may lead to redness, itching, or irritation.
Proper personal protective equipment (PPE) should be used when handling these enzymes.

Inhalation of Peptidases-containing dust or aerosols may lead to respiratory sensitization in some individuals.
Adequate ventilation and respiratory protection may be necessary in situations where aerosols are generated.
Some individuals may develop allergic reactions to Peptidases.

Sensitization to these enzymes can occur through repeated exposure, and individuals with a history of allergies or asthma may be more susceptible.
Ingestion of Peptidases can lead to irritation and sensitization in the gastrointestinal tract.
This is relevant in industries where workers may be exposed to Peptidases-containing substances.

Workers in industries such as biotechnology, pharmaceuticals, and food processing may face occupational exposure to Peptidases.
Proper safety measures, including training, PPE, and engineering controls, should be implemented to minimize risks.
In some applications, such as biocatalysis or protein engineering, Peptidases may be used to catalyze specific reactions.

Identifiers of Peptidases:
Chemical Name: Peptidases
CBNumber: CB5670040
Molecular Weight: 0
MDL Number: MFCD01940183

Properties of Peptidases:
storage temp.: 2-8°C
solubility: H2O: 5-20 mg/mL
form: powder
color: white
FDA 21 CFR: 310.545
EWG's Food Scores: 1

Solubility: H2O: 5-20mg/mL
Appearance: powder
Color: white
Storage Condition: 2-8°C

Specifications of Peptidases:
Appearance: White powder
Assay: 99% min