what are the products of chymotrypsin

Chymotrypsin yielded three major products that were yellow but distinguishable by SDS-PAGE. They were readily separated by DEAE-Sepharose column chromatography. Protein sequencing and mass spectrometry demonstrated that chymotrypsin cleaved the N-terminal 6, 15, or 23 amino acids (T6, T15, and T23).

Full Answer

What is chymotrypsin?

Chymotrypsin is an enzyme. An enzyme is a substance that speeds up certain chemical reactions in the body. People use chymotrypsin to make medicine.

What are the substrates of chymotrypsin?

The main substrates of chymotrypsin are peptide bonds in which the amino acid N-terminal to the bond is a tryptophan, tyrosine, phenylalanine, or leucine. Like many proteases, chymotrypsin also hydrolyses amide bonds in vitro, a virtue that enabled the use of substrate analogs such as N-acetyl-L-phenylalanine p-nitrophenyl amide for enzyme assays.

Which amino acids does chymotrypsin cleave?

Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid C-terminal to the scissile amide bond (the P 1 position) is a large hydrophobic amino acid ( tyrosine, tryptophan, and phenylalanine ).

How do you make chymotrypsin?

Chymotrypsin is formed by the cleavage of several peptide bonds in the inactive monomeric protein, chymotrypsinogen, which is synthesized and secreted by mammalian pancreas. The active enzyme thus produced consists of three nonidentical polypeptide chains (section 5.1.2 ).

What is the substrate and product of chymotrypsin?

The main substrates of chymotrypsin are peptide bonds in which the amino acid N-terminal to the bond is a tryptophan, tyrosine, phenylalanine, or leucine.

Where is chymotrypsin produce?

the pancreasChymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen. α-Chymotrypsin is the predominant form of active enzyme produced from it's zymogen, Chymotrypsinogen A.

What are the products of trypsin action?

The products of trypsin digestion are amino acids and various polypeptides.

What do chymotrypsin break down?

Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid ( ...

What is the role of chymotrypsin?

Trypsin:chymotrypsin is a widely used oral proteolytic enzyme combination to hasten repair of traumatic, surgical, and orthopedic injuries. It shows high bioavailability without losing its biological activities as an anti-inflammatory, anti-edematous, fibrinolytic, antioxidant, and anti-infective agent.

What is another name for chymotrypsin?

Alpha Chymar (Chymotrypsin ).

What does trypsin and chymotrypsin secrete?

the pancreasTrypsin and chymotrypsin are important digestive enzymes that are secreted by the pancreas as the inactive enzyme precursors trypsinogen and chymotrypsinogen. Trypsin activates itself via positive feedback and converts chymotrypsinogen and other inactive enzymes into their active forms.

What class of enzyme is chymotrypsin?

serine proteasesChymotrypsin is a digestive enzyme belonging to a super family of enzymes called serine proteases.

What is the product of pepsin?

Pepsin is an endopeptidase that initiates the process of protein digestion in the stomach. Pepsin action results in the release of small peptides and amino acids (peptones) that, as noted above, stimulate the release of gastrin from antral G cells; these peptones also stimulate CCK release from duodenal I cells.

What proteins does chymotrypsin break down?

Chymotrypsin (EC 3.4. 21.1) is another serine protease produced by the pancreas that hydrolyzes the peptide bonds of tryptophan, leucine, tyrosine, and phenylalanine.

What is the difference between trypsin and chymotrypsin?

Catalytic mechanisms of these two proteases are similar, but their substrate specificities are different. Trypsin favors basic residues like lysine and arginine; chymotrypsin favors aromatic residues like phenylalanine, tyrosine, and tryptophan (14).

What nutrient is digested by chymotrypsin?

Chymotrypsin is a digestive enzyme that breaks down protein in the duodenum of the small intestine. It is initially made in the pancreas as an inactive enzyme called chymotrypsinogen.

Where are trypsin and chymotrypsin produced?

the pancreasTrypsin and chymotrypsin are substances released from the pancreas during normal digestion.

What cells produces chymotrypsin?

The proteolytic enzymes of the digestive tract, including chymotrypsin, trypsin (see Chapter 575) and elastase (see Chapter 584), are produced in inactive forms by the acinar cells of the pancreas, and they are carried as such by the pancreatic juice into the duodenum where they are activated.

Where is chymotrypsin active in the body?

Chymotrypsin is a digestive enzyme synthesized in the pancreas that plays an essential role in proteolysis, or the breakdown of proteins and polypeptides. As a component in the pancreatic juice, chymotrypsin aids in the digestion of proteins in the duodenum by preferentially cleaving peptide amide bonds.

What produces trypsin and chymotrypsin?

Trypsin and chymotrypsin are important digestive enzymes that are secreted by the pancreas as the inactive enzyme precursors trypsinogen and chymotrypsinogen.

Why do people use chymotrypsin?

People use chymotrypsin to make medicine. People use chymotrypsin for redness and swelling associated with pockets of infection (abscesses), ulcers, surgery, or critical illness (trauma), as well as many other conditions, but there is no good scientific evidence to support these uses.

What are the conditions that can cause chymotrypsin to be effective?

Asthma. Swelling ( inflammation) of the main airways in the lung ( bronchitis ). Cough. Critical illness ( trauma). Sinus infections. Skin conditions such as abscesses and ulcers. Wound healing. Other conditions. More evidence is needed to rate the effectiveness of chymotrypsin for these uses.

How long can you take chymotrypsin?

Doses up to 800,000 units per day of this combination have been used safely for up to 10 days. Rarely, chymotrypsin might cause an allergic reaction when taken by mouth.

Is chymotrypsin safe for eyes?

Side Effects. When used in the eye: Chymotrypsin is LIKELY SAFE when used as a prescription medicine in the eye by a healthcare professional. Chymotrypsin can cause side effects when used in the eye, including an increase in pressure in the eye and other eye conditions. When taken by mouth: Chymotrypsin is POSSIBLY SAFE for most people ...

Is chymotrypsin safe for breast feeding?

Symptoms include itching, shortness of breath, swelling of the lips or throat, shock, loss of consciousness, and death. Pregnancy and breast -feeding: There isn't enough reliable information to know if chymotrypsin is safe to use when pregnant or breast-feeding. Stay on the safe side and avoid use.

Does trypsin cause burns?

Burns. There is some evidence that taking a mixture of chymotrypsin and trypsin by mouth might decrease tissue destruction in burn patients. Chronic pain and swelling ( inflammation) of salivary glands (chronic obstructive parotitis).

What is the function of chymotrypsin?

Chymotrypsin (EC 3.4.21.1) preferentially cleaves protein chains at the carboxyl side of aromatic amino acids. Insect chymotrypsins usually have molecular masses of 20–30 kDa and pH optima of 8–11, and they differ from their vertebrate counterparts in their instability at acidic pH, inhibition pattern with SBTI ( Terra and Ferreira, 1994 ), and, finally, in reacting with N-α-tosyl-l-phenylalanine chloromethyl ketone (TPCK) (see below). The distribution of chymotrypsin among insect taxa is similar to that of trypsin ( Terra and Ferreira, 1994 ), including the occurrence in the salivary glands of some heteropteran bugs ( Colebatch et al., 2002 ). The earlier failure to detect chymotrypsin activity in insect midguts was a consequence of using mammalian chymotrypsin substrates, such as benzoyl-tyrosine p-nitroanilide (B-Y-pNA) or benzoyl-tyrosine ethyl ester (B-Y-ee), in the assays. Insect chymotrypsins prefer Phe at P 1, and are almost inactive if Tyr is at that position ( Lopes et al., 2009 ). Furthermore, insect chymotrypsins have an extended active site (as in mammalian chymotrypsin; see Lopes et al., 2009) and larger substrates, like succinyl-AAPF-p-nitroanilide (Suc-AAPF-pNA), are usually necessary for their detection ( Lee and Anstee, 1995; Lopes et al., 2009) ( Figure 8 ). Insect chymotrypsins are usually purified by affinity chromatography in phenyl butylamina-Sepharose (elution with phenyl butylamina) or in SBTI-Sepharose (elution with benzamidine) for enzymes from lepidopterans, and by ion-exchange chromatography for those from dictyopterans, orthopterans, hymenopterans, and dipterans. They have been purified from several sources: Hemiptera ( Colebatch et al., 2002 ), Coleoptera ( Oliveira-Neto et al., 2004; Elpidina et al., 2005 ), Hymenoptera ( Whitworth et al., 1998 ), Siphonaptera ( Gaines et al., 1999 ), Diptera ( de Almeida et al., 2003; Ramalho-Ortigão et al., 2003 ), and Lepidoptera ( Peterson et al., 1995; Volpicella et al., 2006 ). A large number of sequences is also available for insect chymotrypsins at GenBank. All the sequences have a signal peptide, an activation peptide (ending with an arginine residue), the catalytic triad (His 57, Asp 102, and Ser 195), three pairs of conserved cysteine residues, conserved N-terminal sequence IVGG, and Ser/Gly/Tyr 189, which confers specificity to chymotrypsin-like enzymes ( Figure 5 ).

How is chymotrypsin formed?

Chymotrypsin is formed by the cleavage of several peptide bonds in the inactive monomeric protein, chymotrypsinogen, which is synthesized and secreted by mammalian pancreas. The active enzyme thus produced consists of three nonidentical polypeptide chains (section 5.1.2 ).

What is the reaction of chymotrypsin and diisopropylfluorophosphat?

Chymotrypsin reacts stoichiometrically with diisopropylfluorophosphate (DFP) to form an inactive diisopropylphosphoryl enzyme. Amino acid sequence studies have shown that a particular serine residue, later identified as Ser195, becomes phosphorylated in the reaction. Like DFP, phenylmethane sulfonylfluoride (PMSF) is a useful inhibitor that reacts with the same serine side chain. The active site serine also reacts with esters, amides, and peptides. The hydrolysis of such substrates proceeds in two distinct steps, as first demonstrated with p -nitrophenyl acetate. The liberation of p -nitrophenol in the hydrolysis is biphasic: at high enzyme concentration there is a rapid burst of p -nitrophenol product, followed by a slow steady state reaction. The burst reaction was rationalized in terms of acyl-enzyme (EA) formation with a concomitant release of p -nitrophenol (P 1 product), which is followed by the slow deacylation step, yielding acetate ion (P 2) and free enzyme (E) as shown in Equation 1 [18]. The ES complex is the non-covalent enzyme-substrate (Michaelis) complex, while k2 and k3 are the acylation and deacylation rate constants, respectively.

How is chymotrypsin synthesized?

Chymotrypsin is initially synthesized as a 245 amino acid inactive precursor termed chymotrypsinogen . Activation of chymotrypsinogen involves proteolytic cleavage at two sites. The resultant three chains are held together by five disulfide bonds. The overall chymotrypsin molecule is folded into two domains, each containing six beta strands arranged as antiparallel sheets that form a circular structure known as a beta barrel. The active site residues are far apart in the primary sequence but are brought together in a crevice formed between the two protein domains. The active site of chymotrypsin consists of catalytic triad formed by Aspartate 102 positioned close to histidine 57 and serine 195 ( Figure 2 ).

How does chymotrypsin hydrolyze amide?

The hydrolysis of amide and ester substrates by chymotrypsin is a three-step process in which an enzyme–substrate complex and an acyl enzyme intermediate are formed [21] ( Figure 582.2 ). The first evidence for this mechanism was reported by Hartley & Kilby [22] who observed a rapid initial burst in the liberation of p -nitrophenol when chymotrypsin was mixed with excess p -nitrophenyl acetate or p -nitrophenyl ethyl carbonate. They postulated that initially the ester rapidly acylated the enzyme in a mole-to-mole ratio, and that the rate of subsequent substrate turnover was limited by the slow hydrolytic deacylation of the enzyme. The existence of the acyl enzyme intermediate was ultimately proven by the isolation and crystallization of several stable forms such as indolylacryloyl-chymotrypsin [23], tosyl-chymotrypsin ( 2CHA; [24]) and two photoreversible cinnamoyl-chymotrypsins [25]. This later work is especially interesting because, due to the special structure of the bound inhibitor, light-induced cis–trans isomerization increases the rate of deacylation by several orders of magnitude. Photoirradiaton of the inhibited chymotrypsin crystals triggers deacylation, so that the process can be directly studied by X-ray crystallography [26]. Furthermore, the formation of acyl enzyme intermediates in the pathway of amide hydrolysis was also deduced by nucleophile partitioning experiments [27]. Recently, careful analysis of the X-ray structure of γ -chymotrypsin has revealed that this form is an acyl enzyme complex of α-chymotrypsin with its autolysis product (Dixon & Matthews [28]: structure 1GCT; Dixon et al. [29]: structures 2GCT, 3GCT; Harel et al. [30]: structure 8GCH ). In hexane, the tetrahedral intermediate of the reaction was also observed (Yennawar et al. [31]: 1GCM ).

What is chymotrypsinogen A?

α-Chymotrypsin (EC 3.4.21.1; chymotrypsinogen A) is a “hydrolytic enzyme” member of the super-family of serine proteases, enzymes that hydrolytically cleave peptide bonds utilizing a serine hydroxyl group as a nucleophile at the active site. The most extensively studied is bovine pancreatic chymotrypsin. Other enzymes within this classification include elastase, trypsin, thrombin, choline esterase, and subtilisin (a bacterial protease). The overall reaction is shown in Fig. 9.1. Of special note is that chymotrypsin cleaves peptide bonds that are on the C-terminal side of an amide linkage, which contains an aromatic (Tyr, Phe, and Trp) side chain.

What enzymes cleave peptide bonds?

Chymotrypsin is a member of a family of enzymes that cleave peptide bonds through the action of an active site serine (the serine proteases) [15]. This family includes the pancreatic enzymes chymotrypsin, trypsin, and elastase as well as a variety of other proteases (e.g., cocoonase, thrombin, acrosomal protease, etc.).

What is trypsin and chymotrypsin?

8.9.3.1.3 Trypsin and α -chymotrypsin#N#Both trypsin and α-chymotrypsin are a family of serine proteases, and catalyze the enantioselective hydrolysis of amide and esters. CSPs based on trypsin and α -chymotrypsin were introduced by Thelohan et al. 4 and Wainer et al., 5 respectively. Trypsin-based CSPs can resolve O -, N,O -derivatized amino acids that are substrates of the enzyme. 4 This means that chiral separations are due to the activity of the enzyme, and that the chiral recognition site could be on the enzyme activity site. α-Chymotrypsin-based CSPs can resolve amino acid, amino acid derivatives, dipeptides, and other compounds such as naproxen and aryloxy-propionic acids.24

Where is chymotrypsin synthesized?

Chymotrypsin is synthesized in the pancreas as the zymogen chymotrypsinogen (or pre-chymotrypsin). This is a single polypeptide chain of 245 residues containing five intra-chain disulphide bridges. On passing into the intestine, where proteolytic enzymes are required to digest dietary proteins, chymotrypsinogen is attacked by trypsin. This breaks the peptide bond between arginine-15 and isoleucine-16, producing π-chymotrypsin. Already the molecule has full enzymatic activity, but further changes then take place: a dipeptide is removed from positions 14 and 15 by the action of another molecule of π-chymotrypsin, producing δ-chymotrypsin, and further chymotrypsin digestion removes a dipeptide from positions 147 and 148 to give the final product, α-chymotrypsin (Fig. 5.1 ).

What is the active site of chymotrypsin complexed with the covalent inhibitor?

The active site of chymotrypsin complexed with the covalent inhibitor N-acetyl-Leu-Phe-trifluoromethyl ketone is illustrated in Figure 12. 71 This structure reveals not only the hydrogen bond geometry between the Asp102 and His57 (protonated in this complex), but also between the anionic oxygen of the tetrahedral intermediate and the neutral, very weakly acidic backbone NH groups of Gly193 and Ser195 that constitute the “oxyanion” hole. Each of these hydrogen bonding arrays probably contributes significantly to the overall stabilization that is required to allow the tetrahedral intermediate to be kinetically competent.

What is the mechanism of chymotrypsin catalyzed reaction?

A reasonable mechanism for the chymotrypsin-catalyzed reaction is shown in Figure 13. 8,72, 73 The hydrogen bonding interactions between Asp102 and His57 and also between the carbonyl group of the substrate and the NH groups of the oxyanion hole are likely to be responsible for differential stabilization of the intermediate. In Figure 13, the hydrogen bonds involving the bound substrate are “normal” hydrogen bonds whereas those involving the bound intermediate are stronger (perhaps of the short strong/low barrier type) as the proton affinities of the donor and acceptor atoms become similar (see Section 5.02.7 ).

What are the serinyl proteases?

The serinyl proteases include trypsin, chymotrypsin-A, elastase, thrombin, kallikrein, cathepsins-A, G, and R, factor VII, factors IXa–XIIa; and tissue plasminogen factor. High-resolution x-ray crystallographic structures of this protease family have been determined, including those of thrombin (for a review see Stubbs and Bode175; also see Table 2176–182), factor Xa,183 trypsin, 184 kallikrein-A, 185 and elastase. 186–190 For example, a substrate-based inhibitor of thrombin having a boronic acid, B (OH)2 ( Figure 25), substitution for the scissile amide was determined by x-ray crystallography to form a covalent bond with the active site Ser-195 residue.176 The N-terminal Ac-d-Phe-Pro moiety of this inhibitor binds in a β-sheet-type extended conformation that involves hydrogen-bonds with the enzyme and well-defined hydrophobic and aromatic–aromatic (edge-to-face) stacking interactions. The inhibitor Arg side chain binds in an extended conformation, and the guanidino moiety forms bidentate hydrogen-bonding interactions with an Asp-189 residue at the base of the S1 ‘specificity’ pocket and additional hydrogen-bonds to the enzyme, one of which is mediated through a structural water. Related to the substrate-based peptidomimetic inhibitors of thrombin having C-terminal electrophilic groups (e.g., aldehyde, ketone, and boronic acid), a series of nonpeptide inhibitors devoid of P1 electrophilic functionalization have been successfully advanced, as represented by 52, 70 ), 60, 71 and 113. 182 The design of a highly potent and selective amidinopiperidine-based thrombin inhibitor 113 ( Figure 24) was derived from analysis of the x-ray crystallographic structures of thrombin complexed with inhibitors 52 and 60. The latter two compounds showed different trajectories of their P 1 side chains (i.e., guanidinoalkyl and amidinophenyl moieties, respectively) into the S 1 pocket, which accounts for the observed opposing chiral preferences at the C α -position of the P 1 amino acid residues. Furthermore, the C-terminal cycloalkyl moieties of both 52 and 60 were observed to bind to the so-called inhibitor ‘P-pocket’ (i.e., the P 2 substrate pocket), and these compounds therefore provide a unique model of binding versus the substrate-like conformation adopted by the peptidomimetic inhibitors Ac- d -Phe-Pro-boroArg-OH described above. The design of the novel amidinopiperidine-based inhibitor 113 illustrates a ‘transposition’ of the P-pocket binding group to an N-substituted Gly-β-Asp scaffold.

Which enzymes are closely related to serine proteases?

5.1.2 The serine proteases. The serine proteases chymotrypsin, trypsin and elastase, which are produced in an inactive form by the mammalian pancreas, form a closely related group of enzymes. Although only about 40% of the primary structure is common to all three enzymes, most of the catalytically important amino acid residues correspond exactly.

Which organ secretes endopeptidases?

The exocrine pancreas secretes three endopeptidases ( trypsin, chymotrypsin, and elastase) and two exopeptidases ( carboxypeptidase A and carboxypeptidase B) in inactive forms. Enterokinase on the brush border begins a cascade of activation of the pancreatic enzymes by converting trypsinogen into trypsin.

Where is chymotrypsin made?

He operates a private practice in Santa Monica, California. Chymotrypsin is a digestive proteolytic enzyme produced by the pancreas that is used in the small intestine to help digest proteins. The enzyme is also used to help create medicines and has been used in clinical healthcare settings since the 1960s.

How does trypsin help with wound healing?

Research shows that when used in combination with the enzyme trypsin, it can be applied topically to the skin to remove dead tissue from wounds and expedite healing. 3  The two enzymes work together to reduce inflammation and reduce pain associated with healing.

What enzyme breaks down protein?

If your body isn’t producing enough of this enzyme or other digestive enzym es, you may experience discomfort after eating, such as gassiness, cramping, and abdominal pain. 5 

Why is enzyme used in medicine?

It is known to help to reduce redness and swelling caused by surgery or infection and help promote speedier healing of wounds/ traumatic injury to tissue.

Does chymotrypsin help with swelling?

A study conducted in India found that chymotrypsin may be helpful in expediting hea ling after orthopedic surgery. Patients who were given tablets containing chymotrypsin, experienced a significant reduction in pain, reduced swelling, and wound discharge post-surgery. 4 .

Is chymotrypsin safe to take?

Chymotrypsin is generally safe and does not cause unwanted side effects when taken by mouth to reduce inflammation and redness following surgery or injury, and when applied topically to the skin to help heal wounds and burns. Some people may experience gastrointestinal discomfort, such as gas, diarrhea, constipation, or nausea. 2 .

Is chymotrypsin regulated by the FDA?

Most supplements are not regulated by the U.S. Food and Drug Administration (FDA), so it is important to select a product that is well-reviewed and has dosage and ingredients clearly listed on the label. When buying chymotrypsin supplements, choose a product that lists its potency.

How does chymotrypsin work?

More specifically, chymotrypsin operates through a particular type of ping-pong mechanism called covalent hydrolysis. This means that the enzyme first forms a covalent bond with the target substrate , displacing the more stable moiety into solution . This enzyme-substrate complex is called the enzyme intermediate. The intermediate then reacts with water, which displaces the remaining part of the initial substrate and reforms the initial enzyme.

What is chymotrypsin enzyme?

Kinetics. References. Chymotrypsin is a digestive enzyme belonging to a super family of enzymes called serine proteases. It uses an active serine residue to perform hydrolysis on the C-terminus of the aromatic amino acids of other proteins.

What is the name of the enzyme that reacts with water?

This enzyme-substrate complex is called the enzyme intermediate. The intermediate then reacts with water, which displaces the remaining part of the initial substrate and reforms the initial enzyme. Chymotrypsin, like most enzymes, is specific in the types of substrates with which it reacts.

What enzyme converts a protease into an active form?

Upon secretion into the lumen of the small intestine, it is converted to its active form by another enzyme called trypsin. This dependence of a different enzyme for the activation of a protease is a common way for the body to prevent the digestion of organs and other harmful enzymatic side-effects.

What are the two phases of chymotrypsin?

Chymotrypsin is one of the most studied enzymes due to its two phase kinetics: pre-steady-state and steady state . The study of these two kinetic states gives evidence of the "Ping-Pong" mechanism, the formation of covalent complexes leading to covalent hydrolysis reactions, and the rate of the catalyzed reactions.

Which step describes the initial burst of nitrophenolate seen in Hartley and Kilby’s absorbance?

The first step, which describes the initial burst of nitrophenolate seen in Hartley and Kilby’s absorbance plot, is the fastest. The attack of the nitrophenyl acetate substrate by chymotrypsin immediately cleaves the nitrophenolate moiety and leaves the acetate group attached to chymotrypsin, rendering the enzyme inactive.

What is the role of protease in cleaving polypeptides?

As a protease, it cleaves polypeptides, and its inherent specificity allows it to act only on the carboxy-terminal of aromatic residues. It is a somewhat complicated mechanism, and is best explained in a series of steps. 1.

What is trypsin and chymotrypsin?

08 July, 2011. Trypsin and chymotrypsin are two different but related digestive enzymes produced and released by the pancreas. Both enzymes function within the intestine to help break down large protein molecules that we ingest in the foods we eat.

How many amino acids are in trypsin?

There are 20 different amino acids from which these protein chains are made. The specific site along the protein chain where trypsin is active are those with the amino acids lysine and arginine, two of the smaller amino acids.

How does trypsin break down proteins?

Trypsin helps to break down large protein molecules by cutting protein chains at specific sites. The large protein molecule is actually a chain of smaller units called amino acids which are linked, end to end, in chains hundreds. There are 20 different amino acids from which these protein chains are made. The specific site along the protein chain ...

Which enzyme cuts the larger protein chain?

The enzyme chymotrypsin also cuts the larger protein chain but at different sites from where trypsin cuts. Chymotrypsin makes its cut at positions along the protein chain that contain very large amino acids such as phenylalanine, tyrosine and tryptophan. Otherwise, it is very similar to trypsin.

Can trypsin cause gas?

Medical Use of Trypsin and Chymotrypsin. In some individuals, the production of these digestive enzymes is deficient, resulting in the inability to completely digest food. This can result in abdominal pain, indigestion, gas and malnutrition. This condition is treatable with trypsin and chymotrypsin supplements. 00:00.

Overview

Mechanism of action and kinetics

Activation

See also

Further reading

External links