1. ENZYMES AS BIOCATALYSTS
&
USE OF EXOGENEOUS ENZYMES(
CARBOHYDRATE AND LIPID-TRANSFOMING
ENZYMES)
AVNEET KAUR
317006
FSQM
2. ENZYMES
Proteins functioning as catalysts that speed up
reactions by lowering the activation energy.
Has important traits:
are proteins
are catalysts
exhibit selectivity towards substrates.
Enzymes are specific.
Enzymes provide a specific environment within which a
given reaction is energetically more favorable.
3. MECHANISMS OF ENZYMATIC CATALYSIS
Substrate is changed into product via high energy
transition state.
E + S ES
ES E + P
4. Active sites: clefts or grooves, composed of amino acids
from different parts of the polypeptide .
Co-factor: non protein molecule which carries out
chemical reactions that can not be performed by standard
20 amino acids.
Substrate: reactant in biochemical reaction.
Inhibitors: decrease the rate of enzyme-catalyzed
reactions. Can be competitive(Structurally similar inhibitor
and substrate bind to the same site) or non-
competitive(bind non-covalently and reversibly at the sites
other than the active site).
8. EXOGENEOUS ENZYMES
Enzymes which are present in raw, uncooked food are
called food enzymes to indicate where they come from:
the food itself.
Uses:
• glucose, HFCS
production of food commodities
• beer stabilization, meat tenderization
modification of components
• cheese ripening, juice extraction, faster dough mixing
process improvement
9. CARBOHYDRATE-TRANSFORMING
ENZYMES
Most enzymes are hydrolytic and are collectively referred
to as glycosyl hydrolases or glycosidases.
accounts for about half of enzyme use as processing aids
in the food industry.
functions by either general acid–base catalysis and/or
nucleophilic catalysis.
Types (based on the fate of the anomeric configuration
(α or β) of the hydrolyzed glycosidic bond)
“retaining” or “inverting”,
10.
11. STARCH-TRANSFORMING ENZYMES
α-Amylase
• Hydrolyze
starch into
smaller dextrins
• Make “thin”
starch
suspensions
• Has three
separate
domains
(catalysis,
granular starch
binding site, and
for calcium
binding)
β-Amylase
• exoenzyme that
releases
successive
maltose units
from the
nonreducing
end of a
polysaccharide
chain by
hydrolysis of α-
1,4-glucan
linkages.
Glucoamylase
• produce
glucose from
starch
• Uses : in
alcohol
production,
baking, dental
hygiene, fruit
juicing
• Hydrolyzes 1,4-
α-D-glucose
residues
12. Applications of these include
starch hydrolyses,
bakery industry and
brewery and fermentation.
13. SUGAR TRANSFORMATION AND
APPLICATIONS
• Xylose (glucose) isomerase – used in sweetener
production
Glucose Isomerization
• Glucose oxidase obtained from Aspergillus niger.
• Removes oxygen in liquids or within packages, or
generating gluconic acid.
Glucose Oxidation
• production of soft-centered confections and to produce
artificial honey from sucrose.
Sucrose Hydrolysis (Inversion)
14. LIPID-TRANSFORMING ENZYMES
Lipase:
Act only at the oil–water interface. liberates flavoring
(short-chain) fatty acids from lipids and rearranges
fatty acyl groups along the glycerol backbone.
Used in flavour generation, for example in enzyme
modified cheeses.
Helps in preparation of structured lipids.
Added as dough improvers, which manifests as
increased bread volume, more uniform crumb and
air cell size.
15. Lipoxygenases:
Generally considered to have detrimental effects. One
beneficial use of is to provide oxidizing power during
dough conditioning.
oxidizes unsaturated fatty acids generating oxidizing
conditions that help strengthen the gluten network by
affecting disulfide cross-links within the gluten.
Secondary oxidation reactions -destroy endogenous
carotenoids.
16. Phospholipases:
types: A1, A2, C, and D.
PhospholipaseA2 has potential use as an agent to create
superior lysophospholipid emulsifiers from phospholipid-
rich sources, such as egg yolk.
Added to crude oil during degumming stage to hydrolyze
phospholipids at the sn-2. Important for the removal of
otherwise nonhydratable phospholipids.