Study Set Content:
Meat tenderizer
Bromelain
Additive to detergent for removal of protein stains
Alcalase
Whitening of bread
Lipoxygenase:
Produces flavor in cheese
Lipase:
Enzymes lower (blank) , of a particular reaction.
the activation energy, Ea
is the minimum energy needed for a reaction to occur.
activation energy
An enzyme has a high affinity for the t
transition state
An enzyme has a high affinity for the transition state (even higher than for its
substrate
Substrate
Transition state
Product
Concentration of ES Burst of ES complexes form
Pre-steady state
ES remains constant. It is formed as quickly as it breaks dowm
Steady state(equilibrium)
Substrate depletes so fewer ES complexes can form
Post-steady state
Rate of product formation
Slow as must first wait for ES to form. Speeds up as ES forms.
Pre-steady state
Constant rate of formation. Faster than pre-steady state
Steady state
Slow as there are fewer ES complexes. Slows down as substrate runs out.
Post-steady state
Two terms that are important within Michaelis-Menten Kinetics are
Vmax –
Km (Michaelis constant)
the maximum rate of reaction when all enzyme active sites are saturated with substrate
Vmax
The substrate concentration that gives half maximal velocity. Km is a measure of the affinity an enzyme has for its substrate, as a lower Km means that less of the substrate is required to reach half of Vmax.
Km (Michaelis constant
