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Six major classes of enzymes

• Ligase requires ATP and string nucleotides together in nucleic acids and
simple sugars in polysaccharides.

• Lyase breaks bonds between carbon atoms or between carbon and nitrogen.
For example, deaminase removes amino group from amino acid.

• Hydrolase breaks large molecules into simpler molecules with the addition of
a water molecule. For example, proteases split proteins into amino acids;
amylase splits carbohydrates into simple sugars; and lipase breaks apart
triglycerides.

• Transferase removes a part of one molecule and attaches it to another. For


example, transaminase transfers an amino group from an amino acid.

• Isomerase rearranges the atoms in a molecule without changing the chemical


formula. It is important in preparing some carbohydrates for enzymatic
processing.

• Oxido-reductase removes hydrogen or electrons from one molecule and gives


them to another. They are involved in mitochondrial energy production.

• Kinase attaches a phosphate group with a high-energy bond. It is essential for


ATP production and the activation of some enzymes.

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Three major types of enzymes

• Food enzymes are found in raw foods. All food, whether animal or plant,
contains enzymes.

• Digestive enzymes are secreted by the body to digest the food eaten. There
are three categories of digestive enzymes:

• Amylases (found in saliva, the pancreas, and intestinal juices) break


down carbohydrates;

• Proteases (found in the stomach, pancreatic, and intestinal juices) help


digest protein;

• Lipases (found in the stomach and pancreatic juices, and in food fats)
aid in fat digestion.

• Metabolic enzymes run all the body organs and systems by performing
various chemical reactions within the body cells. Without them, life would
cease to exist. Two important metabolic enzymes are SOD (superoxide
dismutase, which is an antioxidant and Catalase, which breaks down
hydrogen peroxide, a metabolic waste product, liberating the oxygen for use
in the body.

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Digestive enzymes and their function

• Amylase I and II are secreted, first by the salivary glands, and then by the
pancreas. They function best in a pH of 6.7-7.5, breaking bonds between
carbohydrate molecules to produce disaccharides and trisaccharides. Amylase
I is activated by chewing and begins the digestive process by converting
starch (amylose) to maltose. Amylase II, produced by the pancreas, is only
slightly different chemically and continues the process started by the salivary
amylase.

• Pepsin is secreted as proenzyme pepsinogen by the chief cells of the stomach


and activated by hydrogen in the stomach acid, also producing hydrochloric
acid at the same time. It functions best in a pH of 1.5-2.0 in order to break
bonds between amino acids in proteins, producing short-chain polypeptides
and destroying any pathogens that enter with the food.

• Trypsin is secreted from the pancreas as proenzyme trypsinogen. It functions


best in a pH of 7-8. Trypsin acts on proteins and polypeptides to produce
short-chain peptides. It also activates other pancreatic proteinases.

• Chymotrypsin is secreted by the pancreas as proenzyme chymotrypsinogen.


It functions best in a pH of 7-8. Chymotrypsin acts on proteins and
polypeptides to produce short-chain peptides.

• Carboxypeptidase is secreted by the pancreas as proenzyme


procarboxypeptidase. It functions best in a pH of 7-8. Carboxypeptidase acts
on proteins and polypeptides to produce short-chain peptides and amino
acids.

• Elastase is secreted by the pancreas as proenzyme proelastase. It functions


best in a pH of 7-8. Elastase targets elastin to produce short-chain peptides.

• Lipase is secreted by the pancreas -- but only if bile salts are present. It
functions best in a pH of 7-8. Lipase targets triglycerides to produce fatty
acids and monoglycerides. Lipase also seems to be activated by the presence
of Vitamin C, glutathione, and cysteine.

• Nuclease is secreted by the pancreas. It functions best in a pH of 7-8.


Nuclease targets nucleic acids RNA and DNA to produce nitrogen bases and
simple sugars.

• Enterokinase is secreted by the mucosal cells of the small intestine and


reaches the lumen through disintegration of shed epithelial cells. It functions
best in a pH of 7-8. Enterokinase targets trypsinogen, a proenzyme, to
produce trypsin.

• Maltase, sucrase, and lactase are secreted by the mucosal cells of the small
intestine and found in the membrane surface of microvilli. They function best
in a pH of 7-8. They respectively target the sugars maltose, sucrose, and
lactose to produce monosaccharides.

• Peptidase is secreted by the mucosal cells of the small intestine and found in
membrane surfaces of the microvilli. It functions best in a pH of 7-8.
Peptidase targets dipeptides and tripeptides to produce amino acids.
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Other common enzymes

• Bromelain is found in pineapple. It is a digestive enzyme that breaks down


protein. It also has anti-inflammatory properties and has proven effective in
treating rheumatoid arthritis and osteoporosis. It also improved mobility while
decreasing pain and joint swelling. Bromelain also breaks down the
fat/cholesterol casings that surround a clot and can “clean up” arterial plaque.
By eating raw pineapple, cardiac function can improve, as well as symptoms
of CHF (congestive heart failure). However, too many people take aspirin for
this purpose, which only prevents the clumping of clots in the blood. It does
not prevent the accumulation of the fats that cause atherosclerosis.
Note that the enzyme is found only in fresh pineapple and is destroyed in
canning or freezing.

• Papain is found in papaya. It is often used with bromelain. Both are used as
meat-tenderizers and to help with protein digestion and in controlling acidic
conditions of the stomach.

• Rennin is found only in the stomachs of infants. It is a milk-clotting enzyme.


Rennin readies the milk for the action of pepsin in breaking down the proteins
and for lipase to break down the fats.

• Pancreatin is usually obtained from an animal source. It is unique because it


possesses proteolytic, lipolytic, and amylolytic properties: proteolytic enzymes
(chymotrypsins, trypsins, pancreato- and carboxypeptidases), amylases,
lipases, phospholipases, as well as nucleic acids (RNA and DNA). It is most
active in a pH of 6.5 to 9.0. It is mainly used when there is pancreatic
insufficiency, inadequate secretions of exocrine pancreas, disturbed digestion
after gastrectomy, and in children with cystic fibrosis.

• Trypsin also comes from an animal source, usually ox pancreas. It has


endoproteolytic properties and splits peptides, amides, and esters. It is most
active in a pH of 7.0 to 9.0 and often used in the debridement of necrotising
wounds, ulcerations, abscesses, empyemas, hematomas, fistulas, and
decubitus ulcers. It can be used internally or externally to accelerate healing
in injuries, inflammations, phlogistic edemas, and traumatic changes as well
as an auxilary agent in meningitis therapy.

• Chymotrypsin is another one from an animal source, usually ox and pork


pancreas. It has endoproteolytic activities, splitting peptides, amides, esters,
and other amino acid-containing compounds. It is most active in a pH of 8.0
and used in the debridement and treatment of abscesses and ulcerations, as
well as in the liquefaction of mucous secretions, in ophthalmic cataract
surgeries and therapy of eyeball hematomas and ophthalmorrhagias, and in
before and after tooth extractions, as well as other forms of dentistry.
Chymotrysin has been used after episiotomy surgeries, as an anthelmintic
agent against enterozoic worms, in early recognition of tumor cells, and in
histologic gastroenterologic diagnostics.

• Papain is obtained from papaya latex of Carica papaya. It splits peptides,


amides, and esters and is most active in a pH of 2.5 to 7.0. It is used in
ophthalmology to prevent cornea scar malformation, intoxications caused by
stings of jellyfish and insects, malabsorption syndromes like gluten
intolerance, treating phlogistic edemas, inflammatory processes, and in
accelerating wound healing.

• Bromelain is obtained from pineapple stems of Ananas comosus and is a


mixture of bromelain A and B, two sulfur-containing proteinases that split
peptides, amides, and glycine esters. It is most active in a pH of 3.0 to 8.0
and used as an adjuvant in treatment of swelling and inflammations caused
by injury and surgery, as well as for painful menstrual hemorrhages, such
boxing injuries as facial swellings and hematomas, acute sinusitis, and in
thromboembolism of central retinal vessels.

• Amylase is obtained from a fungal source, usually from Aspergillus oryzae. It


requires calcium ions for its activity on starch, glycogen, and related poly-
and oligosaccharides. It is most active at a pH of 6.5 and used with other
enzymes as a digestant.

• Lipase is obtained from a fungal source, usually from Aspergillus oryzae. It


depends on calcium ions for its activity of splitting emulsified neutral fats into
fatty acids and glycerol. It is most active in a pH of 5.0 to 7.5 and used to
increase pancreatic and lipolytic activities in pancreatin-containing remedies.
It reduces fat levels in stools when given in combined preparations with
pancreatin. It also intensifies syngergistically biocatalytic activity of
lipoprotein-lipase in the blood and the migration of agranulocytes.

• Lactase is obtained from a fungal source Aspergillus niger and a yeast source
Saccharomyces lactis. A. niger is most active in a pH of 4.0 to 5.0, while S.
lactis prefers 6.0 to 8.5. Lactase is used to treat lactose insufficiency and as a
digestive aide.

• Cellulase is obtained from a fungal source, usually Aspergillus niger. It breaks


down cellulose and cereal glucans and used as a digestive aid. (Cichoke)