Fundamentals of food enzymes Flashcards

1
Q

what are enzymes

A

complex globular protein catalysts
-accelerate the chemical reaction rate
-exist in almost all living systems, needed for metabolism

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2
Q

activity of an enzyme depends on

A

the species/source
-different foods have a different matrix resulting in a different function

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3
Q

why is knowledge of enzyme activity important

A

shelf life
behaviour of a product

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4
Q

what is the active site of a protein

A

location or portion of enzymes consisting of a binding site at which a chemical reaction occurs

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5
Q

who proposed the lock and key theory and explain it

A

fischer 1894
substrates fits like a key to binding site on protein

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6
Q

who proposed induced fit and explain it

A

Koshland 1965
dissimilar molecules can also be a substrate for the same protein, less rigid
active site is more flexible

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7
Q

what is a cofactor

A

participate directly in reactions or serve as an activator

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8
Q

why are enzyme in food different to regular chemistry

A

enzymes are not in isolation
-they are found with the substrate

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9
Q

what is found in the food matrix

A

enzymes
enzyme inhibitors
enzyme-substrate interactions
reaction products
co-factor/coenzymes
substrate
enzyme inhibitor interactions

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10
Q

what is an enzyme inhibitor

A

compound that decreases rate of enzyme-catalysed reactions

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11
Q

what can enzyme inihibitors react with

A

enzyme
enzyme-substrate complex
both

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12
Q

two classes of inhibitors

A

reversible
irreversible

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13
Q

what is enzyme activity dependant on

A

purity
location
environmental properties
Prescence of other factors
stability of enzyme

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14
Q

what effects enzyme specificity

A

bond
group
absolute specificity

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15
Q

name three types of inhibitors

A

competitive
uncompetitive
non-competitive

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16
Q

what are competitive inhibitors

A

react with the enzyme

17
Q

what are uncompetitive inhibitors

A

react with enzyme-substrate complex

18
Q

what are non-competitive inhibitors

A

react with both the enzyme and ES complex

19
Q

what influences enzyme activity

A

intrinsic: pH, substrate, cofactors, inhibitors, activators, buffer concentrations, ionic strength, water activity
extrinsic: temp, pressure, time exposure

20
Q

what is enzyme stability dependant on

A

sources
varieties
purification steps

21
Q

denaturation vs inactivation

A

denaturation: protein structure alteration
inactivation: loss of enzyme activity not necessarily due to denaturation

22
Q

temp range for most enzymes

A

30-40C

23
Q

when do most enzyme begin to denature

A

45C

24
Q

how can ice inactivate

A

ice changes structure
-may still be active before freezing so need to think how fast a thick product might freeze

25
Q

factors that affect enzyme behaviours in partially frozen systems

A

composition of medium
freezing rate
viscosity
sample complexity
phase changes

26
Q

how does viscosity in frozen systems impact enzyme activity

A

viscosity is high, diffusion rate is decreased

27
Q

enzymes that can be damaged by cold denaturation

A

catalase
lactate dehydrogenase

28
Q

effect of pH on enzymes

A

extreme pH may = denaturation
velocity of reaction
affinity of substrate to enzyme
stability of enzyme

29
Q

optimal pH of most enzymes

A

4.5-8

30
Q

optimal pH of pepsin

A

1.8

31
Q

optimal pH of arginase

A

10

32
Q

effect of water activity

A

water serves as a medium for reaction and vehicle for substrate
-still active at dry conditions but rate of reaction is limited by rate of diffusion

33
Q

effect of ionic strength

A

changes solubility of protein
-salting in/out, protein participation

34
Q

what is the michaelis-menten reaction used for

A

time course of enzyme-catalysed reactions

35
Q

y axis of MM reaction graph

A

intial velocity

36
Q

x axis of MM reaction graph

A

substrate concentration

37
Q

when can maximum velocity be acheived

A

when there is a saturated substrate solution

38
Q

what happens to the velocity during the reaction and why

A

it decreases as substrate is depleted

39
Q
A