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  2. Pancreatic enzymes (medication) - Wikipedia

    en.wikipedia.org/wiki/Pancreatic_enzymes...

    A similar mixture of enzymes is sold as pancrelipase, which contains more active lipase enzyme than does pancreatin. The trypsin found in pancreatin works to hydrolyze proteins into oligopeptides; amylase hydrolyzes starches into oligosaccharides and the disaccharide maltose; and lipase hydrolyzes triglycerides into fatty acids and glycerols.

  3. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...

  4. Digestive enzyme - Wikipedia

    en.wikipedia.org/wiki/Digestive_enzyme

    Amylase, produced by the salivary glands, breaks complex carbohydrates, mainly cooked starch, to smaller chains, or even simple sugars. It is sometimes referred to as ptyalin . Lysozyme : Considering that food contains more than just essential nutrients, e.g. bacteria or viruses, the lysozyme offers a limited and non-specific, yet beneficial ...

  5. Lipase - Wikipedia

    en.wikipedia.org/wiki/Lipase

    In biochemistry, lipase (/ ˈ l aɪ p eɪ s, ˈ l aɪ p eɪ z / LY-payss, LY-payz) refers to a class of enzymes that catalyzes the hydrolysis of fats. Some lipases display broad substrate scope including esters of cholesterol , phospholipids , and of lipid-soluble vitamins [ 1 ] [ 2 ] and sphingomyelinases ; [ 3 ] however, these are usually ...

  6. Amylase - Wikipedia

    en.wikipedia.org/wiki/Amylase

    Another form of amylase, β-amylase (EC 3.2.1.2 ) (alternative names: 1,4-α-D-glucan maltohydrolase; glycogenase; saccharogen amylase) is also synthesized by bacteria, fungi, and plants. Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units at a

  7. Trypsinogen - Wikipedia

    en.wikipedia.org/wiki/Trypsinogen

    Trypsinogen (/ ˌ t r ɪ p ˈ s ɪ n ə dʒ ə n,-ˌ dʒ ɛ n / [1] [2]) is the precursor form (or zymogen) of trypsin, a digestive enzyme.It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen.

  8. α-Amylase - Wikipedia

    en.wikipedia.org/wiki/Α-Amylase

    α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2]

  9. Protease - Wikipedia

    en.wikipedia.org/wiki/Protease

    Ribbon diagram of a protease (TEV protease) complexed with its peptide substrate in black with catalytic residues in red.(. A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2]