8 Enzyme Flashcards
enzyme classes
Oxidoreductase
Transferase
Hydrolase
Lyases
Isomerase
Ligase
oxidoreductase
catalayzes oxidation and reduction.
oxidase: catalase, peroxidase, tyrosinase, ascorbic acid oxidase, lipoxygenase
dehydrogenase: acting on hydrogen as donor: succinate dehydrogenase, lactic dehydrogenase
succinate dehydrogenase
breaks glutamic acid into ketoglutaric acid and NH3
lactic dehydrogenase
breaks lactic acid to pyruvic acid
transferase
transfer radical or functional group
hydrolase
catalyze hydrolysis or breaking of substrate by involving water
lipase, glycosidase, aminopeptidase (protease), urease
- lipase: hydrolyzes ester bond in glyceride to produce glycerol and fatty acid
- glycosidase: hydrolyzes glycosidic bond in glycoside
isomerase
atom rearrangement produces isomer.
aldose-ketose isomerization
corn syrup production using isomerase (glucose to fructose)
bromelain facilitates hydrolysis of protein
hydrolysis cuts molecule by adding water
collagen protein + H2O -> pake bromelain -> amino acid
meat tenderizer
lock and key
so specific, active site of enzyme complements the shape of the specific substrate before binding
induced fit model
shape of the active site complements shape of specific substrate right after binding
factors affecting enzyme activity
- environmental conditions
- substrate concentration
- cofactors and coenzymes
- enzyme inhibitors
enzyme inhibitor such as a-glucosidase inhibited by phenol, oxalic acid inhibit succinate
environmental conditions
temperature, pH, Aw, ionic concentration
optimum temperature for enzyme 45-55
most enzyme optimum at 30c, fully denatures at 70c
optimum pH of enzyme activity 4.5-8
effect of pH on enzyme activity
extreme pH level causes denaturation -> structure of enzyme is changed -> active site is distorted
at low Aw (0.2), mobile water isn’t available. enzymatic reactions tend to be surpressed in the lower regions of sorption isotherm. higher Aw is preferred
lipoxygenase in soybean causes off flavor activated after water addition
salting in increases enzyme solubility -> increases activity
salting out decreases enzyme solubility, decreases acttivity
allosteric enzymes have additional site beside active site (allosteric site)
binding of non-substrate molecule to allosteric site functions to influences the activity of the enzyme (allosteric modulator)
allosteric activator: increase E activity
Impair E activity: allosteric inhibitor
binding of substrate to an enzyme’s active site affects the binding of substrate to other active sites
sigmoidal curve
MSG production by corynebacterium glutamicum with the aid of allosteric enzyme
types of inhibition
competitive, noncompetitive, uncompetitive, irreversible
irreversible inhibition”
binds irreversibly through covalent bond, permanently inactivating the enzyme. Vmax decreaes, Km stays.
lipoxigenase enzyme is inhibited by
enzyme inactivation, low pH, fat extraction
shorter chain of protein means great thickening ability. longer chain isn’t good to thicken food product.
concentration of sugar in wheat flour is limited -> addition a-amylase hydrolize amylose which produces maltose for fermentation -> saccharomyces cereviceae to increase CO2 and ethanol production 0> hgiher volume and bigger size