Enzymes - Supercatalysts
- Discovery
- Spallanzani (1780) - digestive juices of birds break down meat
- Berzelius (1836) - fermentation must involve catalysis
- Wohler (1828) - chemical synthesis of urea
- Buchner (1897) - cell-free, enzymatic fermentation
- Northrop (1930) - enzymes are proteins
- Terms
- Substrate - molecule acted on by enzyme
- Active site - location in the enzyme where the reaction catalysis occurs
- Specificity
- Speed increase by up to a trillion fold
- Specific for substrates (molecules enzymes work on) - Box 2.1
- Lock and Key (Fischer)
- Induced fit (Koshland) - Figure 2.6
- Structures
- 20 amino acids
- Disulfide bonds (between cysteines)
- Hydrogen bonds
- Hydrophobic amino acids "inside" enzyme
- Hydrophilic amino acids "outside" enzyme
- Enzyme Classes
- Coenzymes
- Ions - Fe, Mg, Mn, Zn
- Vitamin precursors - NAD, FAD
- Lysozyme
- Industrial enzyme production
- Animals - pepsin, trypsin, chymotrypsin, lipases, amylases
- Plants - papain
- Microbes - thermophiles
- Energetic Mechanism
- Lowered activation energy - Box 2.5
- Enzymes
- Amylases - breakdown of carbohydrates in grain
- Pectinases - breakdown of pectins in fruits and vegetables
- Biodetergents - hydrolytic enzymes / subtilisin
- Proteases - tenderizing beef (papain) (Figure 2.18)
- Serine Proteases (Figure 2.17)
- Technologies
- Immobilizing enzymes
- Protein engineering
- Subtilisin (Box 2.9 showing oxidation)
- Immobilizing cells (Figure 2.36)
- Enzyme membrane reactors (Figure 2.37)