s2 l6 pharmaceutical uses of enzymes l.
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S2 L6 Pharmaceutical uses of enzymes. Anna Drew. Enzymes. catalyse (speed up) chemical reactions involved in most processes in a biological cell proteins specific activity affected by other molecules (inhibitors) temperature chemical environment (pH) concentration of substrate

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enzymes
Enzymes
  • catalyse (speed up) chemical reactions
  • involved in most processes in a biological cell
  • proteins
  • specific
  • activity affected by
      • other molecules (inhibitors)
      • temperature
      • chemical environment (pH)
      • concentration of substrate
  • wide range of uses
      • household products
      • pharmaceutical
papain
Papain
  • Cystine protease hydrolase enzyme
  • Source:
    • Papaya (Carica papaya)
    • Mountain papaya (Vasconcellea cundinamarcensis)
      • latex from the neck of fruit is collected, dried to form crude material
      • extraction process to purify to powder or liquid form
      • also contains chymopapain
  • Use: anti-inflammatory and digestive
    • meat tenderiser
      • breaks down tough meat fibres
      • long traditional use in S.American
    • teeth whitening agent
      • In some toothpastes
    • contact lens cleaner
    • jellyfish, bee/wasp stings, stingray wounds (home remedy)
      • breaks down protein toxins in the venom
    • wound debriding
    • digestive aid
bromelain
Bromelain
  • One of two proteases
      • Stem bromelain
      • Fruit bromelain
  • History:
      • 1891 isolated
      • 1957 introduced as therapeutic supplement
      • 13th most widely used herbal medicine in Germany
  • Source: Bromeliaceae family
      • eg pineapple Ananas comosus – commerically from thestem
      • Thailand – after fruit harvesting stem stripped, crushed, pressed to get juice, concentrated
  • Use: meat tenderising
    • anti-inflammatory: sports injury, trauma, arthritis
    • digestive problems, phlebitis, sinusitis
    • platelet clumping, blood clots in arteries
  • A/E: may show cardiotonic activity (doses of up to 1840mg)
    • nausea, vomiting, diarrhoea, menorrhagia, possible allergenic reaction
trypsin chymotrypsin
Trypsin, Chymotrypsin
  • Serine proteases or endopeptidases

– ‘proteolytic’

- hydrolyse peptide bonds

    • modify the electrostatic environment of the serine
      • chymotrypsin -> phenylalanine, tryptophan and tyrosine residues
      • trypsin -> aspartic acid residue (in catalytic pocket) which attracts and stabilises lysine and arginine
    • both have to be activated
    • inactive form trypsinogen
      • removal of hexapeptide from terminal end -> β-trypsin
      • further AA removal -> other forms eg α-trypsin
    • cystic fibrosis – trypsin deficiency
  • Source: bovine pancreas (purified)
      • crystallised from pancreatic juice
      • introduced as medicinals mid-20th century
      • ? dosage forms not available in US
slide6
Uses: (* modern, rest historical)
    • Topical* (ointment, dusts, dressing, gel capsule to insert into fistulas):
      • cleaning necrotic wounds
        • attack dead tissue
        • not living which has inhibitory enzymes
      • cleaning suppurating wounds
        • decreases pus
      • burns – reduces tissue destruction and free radical production
    • Oral:
      • with buccal tablets
      • pancreatic supplement
      • to dissolve blood clots (microbial form)*
      • combined with papain in many cancers to reduce disease and radiation/chemotherapy symptoms*
      • (in baby foods to pre-digest it*)
    • Inhalation (spray): to reduce tenacious sputum
    • I/M: anti-inflammatory (pancreatic form)
    • Injectable:
      • cataract and eye lens surgery* – ocular inflammation
      • phlebitis
      • traumatic wounds
    • Chymotrypsin
        • more anti-inflammatory activity
        • used for sporting wounds
  • C/I: liver disease, blood clotting
pancreatin
Pancreatin
  • Source: porcine pancreas
      • crude form used since before 1870
  • Use: for reduced exocrine secretion
    • pancreatic enzyme supplements - pancrelipase
      • cystic fibrosis
      • pancreatectomy
      • chronic pancreatitis
      • pancreatic cancer (if obstructs outflow)
  • C/I: hypersensitivity to porcine products
  • Products: standardised for lipase, amylase and protease activity
      • fat, carbohydrate and protein digestion
  • Counselling:
    • inactivated by gastric acid
      • best taken with food (immediately before or after)
        • H2antagonists one hour before or concurrent antacids can reduce gastric acidity
        • no chewing enteric-coated preparations
    • inactivated by heat
      • avoid mixing with hot (temperature) food
    • adequate hydration with high-dose formulations
slide8
Pepsin
    • Source: porcine gastric muscosa
    • Use: (protease)
      • gastric hypochlorhydria
      • deficiency of gastric enzymes
      • dyspepsia
  • Diastase
    • Refers to α-,β-,γ-amylase
      • first discovered in 1833 in malt solution
    • Source:
      • Animal: eg porcine
      • Vegetable: mould (Aspergillus oryzae – taka-diastase), malt, bacteria
    • Action: catalyses breakdown of starch to maltose
    • Use: overindulgence in starchy foods
  • Pectinase
    • Action: refers to enzymes that break down pectin
      • polysaccharide substrate found in plant cell walls
      • eg polygalacturonase
    • Source: extracted from fungi
      • eg Aspergillus niger
    • Use: processing involving degradation of plant material
      • to speed up extraction of juice from fruit eg apples
      • retting – obtaining fibres of eg flax, jute, hemp
urokinase
Urokinase
  • Source: isolated from human urine
  • Action:
    • convert plasminogen to plasmin which catalyses the breakdown of fibrin
  • Use:
    • deep vein thrombosis, pulmonary embolism
    • thrombosed IV cannulae, central venous catheters and haemodialysis shunts
    • peripheral arterial thromboembolism
  • A/E: bleeding, allergic reactions, cholesterol embolism
  • C/I: bleeding disorders, history of bleeding
asparaginase
Asparaginase
  • Source: isolated from E.coli
    • recombinant form expressed in the bacteria
  • Action:
    • catalyses the conversion of the AA L-asparagine to L-aspartic acid reducing availability of L-asparagine to leukaemic cells
  • Use:
    • ALL acute lymphoblastic leukaemia
    • some subtypes of non-Hodgkin’s lymphoma
  • A/E: allergy, pancreatitis, coagulopathy
  • C/I: previous allergic reaction to it, pancreatitis
  • Counselling: increase fluid intake and avoid dehydration
hyaluronidase
Hyaluronidase
  • Source:
    • buffalo leeches
      • leeches of the sub-family Hirudinariinae
      • eg Hirudinaria manillensis, Poecilobdella granulosa
    • ? sheep
    • now human recombinant
  • Action: degrades or hydrolyses hyaluronic acid
    • part of the interstitial barrier (connective tissue)
  • Use: speeds dispersion and delivery of drugs
    • ophthalmic surgery with local anaesthetics
    • renders tissues more easily permeable to injected fluids
      • eg by subcutaneous injection – hypodermoclysis
    • extravasation
      • (inadvertant leakage of the drug out of a vein into surrounding tissue)
many other recombinants
Many other recombinants
  • Tissue plasminogen activator (tPA)
    • myocardial infarction, ischaemic stroke, certain pulmonary embolisms
  • DNA-ase
    • liquefy mucopurulent secretions in bronchopulmonary disease
      • from bovine pancreas in 1956 (dornase)
      • now recombinant human for cystic fibrosis
  • Imiglucerase
    • analog of human β-glucocerebrosidase
    • Type I Gaucher disease
  • N-acetyl-galactosamine-4-sulfase
    • mucopolysaccharadosis
  • Alpha-L-iduronidase
    • mucopolysaccharadosis I
  • α-glucosidase
    • Pompe disease (rare)
  • Alpha-1-antitrypsin
    • alpha-1-antitrypsin deficiency (emphysema, liver)
  • enzyme mixture – coeliac disease (gluten)