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FOOD TECHNOLOGY > FCH - Enzymes > Flashcards

FCH - Enzymes Flashcards

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1
Q

Break the chemical bonds in reactants and re-arrange these bonds into products.

A

Chemical Reactions

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2
Q

Absorb of Energy

A

Endothermic

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3
Q

Release of Energy

A

Exothermic

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4
Q

The minimum energy required for a chemical reaction to take place.

A

Activation Energy

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5
Q

Chemical reactions can be speed up at least two ways:

A
  1. Temperature
  2. Catalysts
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6
Q

Speeds up the rate of chemical reactions.

A

Catalysts

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7
Q

Catalysts can either be _____ or _____.

A

Organic or Inorganic

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8
Q

Catalyst that is metals or ionic compounds.

A

Inorganic catalyst

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9
Q

Organic catalysts or ______.

A

Enzymes

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10
Q

Characteristics of Organic catalysts: Enzymes.

A
  1. Enzymes are natural and non-toxic.
  2. Due to its high-specificity enzymes have no side reactions; thus, products of enzymatic process possess no contaminants.
  3. Enzymes are active under mild conditions of temperature and pH; and
  4. Enzymes can be easily inactivated.
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11
Q

Enzymes as biocatalysts possess three important traits:

A
  1. They are proteins.
  2. They are catalysts.
  3. They exhibit selectivity towards substrates.
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12
Q

The most common and ubiquitous form of biological catalyst.

A

Enzymes

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13
Q

They are responsible for life processes and mediate synthetic, turnover, signalling, and metabolic functions.

A

Enzymes

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14
Q

Enzyme History

Egyptian and Sumerians developed fermentation for use in brewing, bread making and cheese making.

A

2000 BC

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15
Q

Enzyme History

Calves’ stomach and the enzyme chymosin used for cheese making.

A

800 BC

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16
Q

Enzyme History

Yeast cells which cause fermentation were identified and the term ‘enzyme’ has first named meaning in yeast in Greek.

A

1878

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17
Q

Enzyme History

Enzymes were shown to be protein.

A

1926

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18
Q

Enzymes history

Enyzme preparation was developed to improved the digestibility and nutrient availability for animal feed.

A

1980

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19
Q

They are present in raw materials and are responsible for the continuous chemical changes that occur in food products.

A

Enzymes

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20
Q

As mentioned enzymes are present in raw materials and are responsible for the continuous chemical changes that occur in food products. Give three examples.

A
  1. Can be suppressed (e.g. sterilizing),
  2. Led in the right direction (cheese making)
  3. Added (exogenous enzymes).
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21
Q

In food systems, enzymes serve as:

A
  • to upgrade product quality,
  • to develop flavors,
  • improve extraction technique
  • increase by-product utilization.
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22
Q

TWO classification of enzymes.

A
  1. Exogenous
  2. Endogenous
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23
Q

This classification of enzymes is added to foods to cause a desirable change.

A

Exogenous

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24
Q

This classification of enzymes can be obtained from a variety of sources.

A

Exogenous

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25
Q

This classification of enzymes choices are based on cost and functionality.

A

Exogenous

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26
Q

What are the appropriate functionality of EXOGENOUS enzymes?

A
  1. Catalytic activity
  2. Selectivity
  3. Stability under the conditions that prevail during the specific application.
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27
Q

This classification of enzymes exist in foods which may or may not be responsible for reactions that affect food quality.

A

Endogenous

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28
Q

This classification of enzymes pose greater challenges to control, since they are present in the food matrix at a range of levels.

A

Endogenous

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29
Q

This classification of enzymes are constraints as to how the foodstuff can be handled to modulate enzyme action.

A

Endogenous

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30
Q

What are the source of enzymes?

A
  1. Edible plants
  2. Animals
  3. Microorganisms
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31
Q

As a source of enzymes, it is the most utilized due to its increased stability and versatility.

A

Microorganisms

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32
Q

Microorganism should not pose this characteristics as a source of enzymes:

A
  1. It should not be pathogenic.
  2. It should not produce toxin.
  3. It should not produce antibiotics that can destroy the enzyme
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33
Q

They are the agents that accelerate the rate of reactions without themselves undergoing any net chemical modification.

A

Catalysts

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34
Q

They function similarly by reducing the energy barrier required for the
transformation of a reactant into a product.

A

Catalysts

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35
Q

Mechanism of Enzyme Action

These are the molecule that binds to the active site of the enzyme.

A

Substrates

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36
Q

Mechanism of Enzyme Action

This is the specific region or location of the enzyme which combines with the substrate.

A

Active site

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37
Q

Mechanism of Enzyme Action

In this model, the enzyme-substrate interaction suggests that the enzyme and the substrate possess specific complementary geometric shapes that fit exactly into one another.

A

Lock-and-key model

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38
Q

Mechanism of Enzyme Action

Like a key into a lock, only the correct size and shape of the substrate (the key) would fit into the active site (the keyhole) of the enzyme (the lock).

A

Lock-and-key model

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39
Q

Mechanism of Enzyme Action

This model suggests that the active site continues to change until the substrate is completely bound to the active site of the enzyme, at which point the final shape and charge is determined.

A

Induced-fit model

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40
Q

Mechanism of Enzyme Action

Unlike the lock-and-key model, the __________ shows that enzymes are rather flexible structures.

A

Induced-fit model

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41
Q

Is the protein part of the enzyme and in most cases inactive or possess no catalytic activity.

A

Apoenzyme

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42
Q

It contains contains a protein part plus a prosthetic group and the active form of the enzyme.

A

Holoenzyme

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43
Q

Are compounds that are indispensable to enzyme action.

A

Prosthetic group

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44
Q

What are the Prosthetic group?

A
  1. Coenzyme
  2. Cofactor
  3. Ligands
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45
Q

Prosthetic group:

The vitamin derived and in most cases water soluble vitamins.

A

Coenzyme

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46
Q

Prosthetic group:

Metals and Minerals

A

Cofactor

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47
Q

Prosthetic group:

Biomolecules such CHO or lipids attached to the protein part of the enzyme.

A

Ligands

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48
Q

Is a group of enzymes that catalyzes a single reaction only. They are multiple in forms and differs in amino acid sequence.

A

Isozymes

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49
Q

Is the part of the enzyme where the chemical reaction occurs. This is also the binding site of the substrate.

A

Active site

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50
Q

These are substances that can either activate or inhibit the enzyme by altering the conformation of the active site.

A

Allosteric factor

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51
Q

Is the study of the rate of enzyme-catalyzed reactions.

A

Enzyme Kinetics

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52
Q

The transitory of molecular structure in which the molecule is no longer a substrate but not yet a product.

A

Transition state

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53
Q

Is the amount of energy needed to bring 1 mole of the reactants to the transition state.

A

Activation energy

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54
Q

What are the 6 groups of enzyme classification and nomenclature?

A
  1. Oxidoreductases (EC 1)
  2. Transferases (EC 2)
  3. Hydrolases (EC 3)
  4. Lyases (EC 4)
  5. Isomerases (EC 5)
  6. Ligases (EC 6)
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55
Q

It catalyze oxidation reduction reactions.

A

Oxidoreductases

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56
Q

Examples of Oxidoreductases

A
  • Polyphenoloxidase
  • Catalase
  • Peroxidase
  • Lipoxygenase
  • Glucose oxidase
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57
Q

It catalyze reactions involving transfer of functional groups.

A

Transferases

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58
Q

Examples of Transferases

A
  • Cyclodestrin glycosyltransferase
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59
Q

It catalyze hydrolytic reactions.

A

Hydrolases

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60
Q

Three kinds of Hydrolases are:

A
  1. Peptide-hydrolases: proteolytic enzymes (e.g. papain).
  2. Glycoside-hydrolases: amylolytic enzymes, cellulases, hemicellulases, invertase.
  3. Ester-hydrolases: pectin-esterase, lipase, chlorophylase, ribonucleas.
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61
Q

It catalyze reactions involving addition of double bonds.

A

Lyases

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62
Q

Examples of Lyases

A
  • Endo-pectate lyase,
  • Endo-pectin lyase
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63
Q

It catalyze isomerization reactions.

A

Isomerases

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64
Q

Example of Isomerases

A
  • Glucose isomerase
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65
Q

It catalyze formation of bonds involving the use of ATP.

A

Ligases

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66
Q

Most restrictive type of specificity. The enzyme will catalyze only one reaction with a specific substrate.

A

Absolute specificity

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67
Q

Example of Absolute specificity

A

urease acts only urea; maltase acts only to maltose

68
Q

The enzyme will act only on molecules that have specific functional groups.

A

Group specificity

69
Q

Example of Group specificity

A

Chymotrypsin – specific on peptide bonds where aromatic groups are attached; trypsin specific only to peptide bonds where basic amino acids are attached.

70
Q

The enzyme will act on a particular type
of chemical bond regardless of the rest of the molecular structure.

A

Linkage specificity

71
Q

Example of Linkage specificity

A

lipase – acts on an ester bond

72
Q

The enzyme will act on a
particular steric or optical isomer.

A

Stereochemical specificity

73
Q

Example of Stereochemical specificity

A

amylase – specific for alpha-linkages

74
Q

What are the 5 enzyme activity and inhibition?

A
  1. Temperature
  2. pH
  3. Substrate concentration
  4. Enzyme concentration
  5. Enzyme inhibitors
75
Q

Temperature

A

Generally most enzymes have optimum temperature at 30 to 40 °C. At higher temperature, activity decreases due to protein denaturation.

76
Q

pH

A

The optimum pH of most food enzymes occurs at a range of 4.5 – 8.0. At extreme pH enzyme is inactivated due to denaturation. However, some enzymes are active at acidic pH such as stomach enzyme pepsin.

Arginase is most active at a basic pH 10.

77
Q

Substrate concentration

A

At lower concentrations, the active sites on most of the enzyme molecules are not filled because there is not much substrate. The maximum velocity of a reaction is reached when the active sites are almost continuously filled. After this point, reaction rate will not increase.

78
Q

Enzyme concentration

A

As the amount of enzyme is increased the rate of reaction increases. If there are more enzyme molecules than are needed, adding additional enzyme will not increase the rate. Reaction rate therefore increases as enzyme concentration increases but then it levels off.

79
Q

Enzyme inhibitors

A

Enzyme inhibitors are substances which alter the catalytic action of the enzyme and consequently slow down, or in some cases, stop catalysis. There are three common types of enzyme inhibition - competitive, non-competitive and substrate inhibition.

80
Q

The enzyme production and use of enzymes is a major part of ____________ industry.

A

Biotechnology

81
Q

The first enzyme produced in 1896 which is a fungal amylase used to cure digestive disorders.

A

Taka- Diastase

82
Q

Sources of enzymes in plants.

A
  1. Bromelain
  2. Esterase
  3. Ficin
83
Q

Sources of Enzymes in animals.

A
  1. Lipase
  2. Pepsin
  3. Rennin
84
Q

Challenges of using plants and animals as source of enzymes.

A
  1. High cost
  2. Difficult to isolate and purify
  3. High risk
85
Q

The most significant and convenient source of commercial enzymes used in the industry.

A

Microorganisms

86
Q

This source of enzyme in microorganisms can produce at least 40 commercial enzymes.

A

Aspergillus Niger

87
Q

What are the 4 steps in microbial production of enzyme?

A
  1. Selection of organism
  2. Formulation of Medium
  3. Production Process - Fermentation
  4. Recovery and Purification
88
Q

In the first step of microbial production of enzyme, selection or organism should be:

A
  • Non-pathogenic cell
  • Less fermentation time
  • Simple isolation and separation
89
Q

In the second step of microbial production of enzyme, formulation of medium should:

A
  • Supports the growth of m/o
  • Medium should be readily available, low cost and nutritionally safe
90
Q

Examples of media that can be used in formulation of medium.

A
  • starch hydrolysate
  • molasses
  • whey
  • casein
  • yeast extract
  • soybean meal
  • wheat
  • peanut
  • corn syrup liquor
91
Q

What are the 2 fermentation in the third step of microbial production of enzyme which is the production process?

A
  1. Submerged culture fermentation (SCF)
  2. Solid state fermentation (SSF)
92
Q

It is commonly used for industrial application for microbes that require high MC.

A

Submerged culture fermentation (SCF)

93
Q

It gives more yield and less chances of infection, and also employs liquid substrate such as broth and molasses.

A

Production process – Fermentation

94
Q

It is used for microbes that require less moisture content for growth. Specifically, for isolation of enzymes from fungi.

A

Solid state fermentation (SSF)

95
Q

The substrates used for this one include bran, bagasse, and paper pulp.

A

Solid state fermentation (SSF)

96
Q

It is less effluent and waste materials can be recycled.

A

Solid state fermentation (SSF)

97
Q

In the third step of microbial production of enzyme, production process -fermentation:

A
  • 2- 7 days
  • Bioreactor should be sterile throughout the fermentation
  • pH, temperature, oxygen supply and nutrient addition must be optimal
  • Batch or continuous
98
Q

In the fourth step of microbial production of enzyme, recovery and purification:

A
  • Depend on the nature of enzyme (crude/ purified, liquid, solid).
  • Isolated enzymes can be precipitated using salts and organic solvents.
  • Separation and purification of enzymes can be done by chromatographic techniques.
99
Q

Defined as the imprisonment of cell or enzyme in a distinct support or matrix.

A

Enzyme Immobilization

100
Q

The first immobilized enzyme was ________________ of Aspergillus oryzae for the production L-amino acids in Japan.

A

Amino acylase

101
Q

Enzyme Immobilization

A
  • Enzymes movement are physically/chemically restricted.
  • Even in small amounts, enzymes achieve high biocatalytic activity.
  • Immobilized enzymes are also economical because they can also be used repeatedly and continuously.
  • The product can be obtained free of the enzyme; thus, of high purity.
102
Q

Why immobilize enzymes?

A
  1. Accelerate the reaction
  2. Specificity and unmodified
  3. Cost-effective
  4. Easy to separate
  5. Can be re-used
103
Q

ADVANTAGES OF IMMOBILIZED ENZYMES

A
  1. Increased functional efficiency
  2. Enhanced reproducibility
  3. Reuse of enzymes
  4. Continuous use
  5. Less labor input
  6. Saes capital const and Investment of the process
  7. Minimum reaction time
  8. Less contamination in products
  9. More stability of products
  10. Stable supply of products
  11. Improved process control
  12. High E:S (enzyme:substrate) ratio
104
Q

DISADVANTAGES OF IMMOBILIZED ENZYMES

A
  1. High cost for the isolation, purification and recovery of active enzyme.
  2. Applications are limited – very few industries use immobilized enzymes.
  3. Catalytic process are reduced and completely lost after immobilization.
  4. Some enzymes become unstable after immobilization.
  5. Enzymes are inactivated by the heat generated in the system.
105
Q

APPLICATION OF IMMOBILIZED ENZYMES

A
  1. Industrial Production
  2. Biomedical Applications
  3. Food Industry
  4. Research
  5. Production of biodiesel
  6. Waste water management
  7. Textile
  8. Detergent
106
Q

It holds the enzyme permanently or temporarily for a period of time. It also should be cheap and easily available.

A

Support or Matrix

107
Q

Characteristics of ideal matrix should be:

A
  • Economical
  • Chemically inert
  • Stable
  • Natural / Synthetic
  • Organic/ Inorganic
  • Enhance enzyme stability
  • Regenerable
108
Q

Support of Matrix: Organic

A
  • Cellulose
  • Dextrans
  • Agar
  • Agarose
  • Chitin and chitosan
  • Alginate
  • Collagen
  • Polyacrylate
  • Polystyrene
109
Q

Support of Matrix: Inorganic

A
  • Zeolites
  • Ceramics
  • Silica
  • Glass
  • Activated carbon
  • Metals
  • Charcoal
110
Q

METHODS OF ENZYME IMMOBILIZATION

A
  1. Binding > Adsorption > Covalent
  2. Physical Retention > Entrapment > Encapsulation
111
Q

In this method of enzyme immobilization, there is a direct physical and/or chemical interaction between the carrier and enzyme.

A

Immobilization by binding

112
Q

In Immobilization by binding, the binding of enzymes to carriers is achieved via _____________ or _________________.

A

adsorption
covalent mechanisms

113
Q

The binding on the surface of the
carrier. It is also the oldest and simplest method of enzyme immobilization.

A

Adsorption

114
Q

In this method of enzyme immobilization, there is no permanent bond formation between matrix and enzyme and it involves weak forces such hydrogen binding and Van der Waals interaction

A

Adsorption

115
Q

Adsorption matrices involves:

A

silica, charcoal, and clay

116
Q

It affects the binding in adsorption.

A

Change in pH, temperature and ionic strength.

117
Q

The binding is through sharing of electrons between the carrier and the enzyme.

A

Covalent

118
Q

It is a permanent method for enzyme immobilization and provides stronger bonds than adsorption.

A

Covalent

119
Q

The active enzyme is covalently bonded with a linking agent.

A

Crosslinking

120
Q

Functional groups that forms covalent bonds:

A
  • Amino group
  • Hydroxyl group
  • Carboxyl group
  • Phenol rings
  • Thiol and methyl thiol groups
121
Q

Immobilization of enzymes is done through matrix entrapment or membrane closures.

A

Immobilization by physical retention

122
Q

In this enzyme immobilization, enzyme is
entrapped in a gel matrix.

A

Matrix entrapment

123
Q

Matrix entrapment

Substrate is passed through a column filled with _______ and the end result is the product.

A

Beads

124
Q

Matrix entrapment

Enzymes are supported on ________ format made up of collagen, cellulose etc.

A

Fiber

125
Q

It is a fast method of enzyme immobilization.

A

Matrix entrapment

126
Q

In this enzyme immobilization, enzymes can move in a well-defined space but is limited.

A

Membrane enclosures

127
Q

It is the formation of a polymer around
the enzyme.

A

Encapsulation

128
Q

It is cheap and simple method of enzyme immobilization and has membrane reactors.

A

Membrane enclosures

129
Q

Significance of Enzymes in the Food Industry:

A

*Produce high quality products
*Low production cost
*Minimal waste
*Minimum energy consumption
*Biodegradability

130
Q

Enzyme are used in the baking industry for:

A

*Dough handling
*Taste
*Color
*Moisture and volume
*Control of overcrumb texture

131
Q

In the baking industry, α-AMYLASE:

A
  • Produce dextrins which are broken down into sugars
  • Flour supplement
  • Anti-staling effect
  • Modifies starch while most starch start to gelatinize
  • Starch granules more flexible during storage
132
Q

In the baking industry, β-AMYLASE:

A
  • Improves yeast fermentation
  • Increases bread volume
133
Q

In the baking industry, MALTOGENIC AMYLASE:

A
  • Breaks down starch into maltose
  • Flour supplement
  • Anti-staling effect
  • Modifies starch while most starch start to gelatinize
  • Starch granules more flexible during storage
134
Q

In the baking industry, LIPOXYGENASE:

A

Used for bread whitening

135
Q

In the baking industry, HEMICELLULASE:

A
  • Improves dough property
  • Decrease stickiness of bread
136
Q

In the baking industry, PENTONASES:

A
  • Improves dough machinability – more stable, flexible and easy to handle dough.
  • Better storage properties
  • Softer crumb
  • Improves volume
137
Q

In the baking industry, PROTEASE AND PROTEINASE:

A
  • Reduces gluten elasticity in biscuits and wafer production
  • Improves elasticity
  • Improves volume
138
Q

In the baking industry, GLUCOSE OXIDASE:

A
  • Oxidizes glucose and produce gluconic acid and hydrogen peroxide.
  • Strengthens cross-links in gluten
139
Q

In the dairy industry, RENNIN (RENNET):

A
  • Extracted from the stomach of young calves
  • Coagulant of milk to become cheese
  • Separates solid curd and liquid whey
  • The common vegetable rennet is “thistle”
140
Q

In the dairy industry, LACTASE:

A
  • Artificially extracted from yeast.
  • Used in the production of lactose free milk, ice cream, sweetened flavored and condensed milk.
141
Q

In the dairy industry, CATALASE:

A
  • Produced from bovine livers and microbial source.
  • Prevent oxidation – breaks down hydrogen peroxide.
142
Q

In the dairy industry, PROTEASE:

A
  • Hydrolyzes specific peptide bond to generate casein in the production of cheese.
  • Used to develop flavor compounds.
143
Q

In the dairy industry, LIPASES:

A
  • Flavor development – increase sweetness
  • Prevent crystallization
  • Fat hydrolysis
144
Q

In the dairy industry, PROTEASE:

A
  • Useful during the malting process
  • Breaks larger protein which enhances the retention of beer
  • Reduces haze
145
Q

In the brewing industry, β- GLUCANASE:

A
  • Aids in filtration after mashing and brewing
  • Breaks down glycosidic bonds within beta-glucan
  • Improves clarification
  • Reduces maturation duration
146
Q

In the brewing industry, α- AMYLASE:

A
  • Converts starch dextrin
  • Solubilized carbohydrates found in barley and other cereals
  • Decreases the time required for mashing
147
Q

In the brewing industry, AMYLOGLUCOSIDASE:

A
  • Caramelization of saccharides
  • Not thermostable
  • Results in product loss and increase in impurities
148
Q

In the meat industry, PROTEASE:

A
  • Bromelain (pineapple), papain (papaya)
  • Immobilized from Bacillus spp with alginate gel as the matix
    (entrapment method)
149
Q

In the meat industry, PAPAIN:

A
  • Found in papaya – latex part
  • Purified and sold in powder or liquid form
  • 95% of meat tenderizer are made from papain
150
Q

In the meat industry, TRANSGLUTAMINASE:

A
  • Induce gelation in meat products
151
Q

In the sugar industry, GLUCOSE ISOMERASE:

A
  • Converts glucose to high fructose corn syrup – sweeter
  • Can come from different source: bacteria, fungi, animal and plant
  • HFCS is a sweetening agent used for carbonated beverage (softdrinks)
152
Q

In the sugar industry, AMYLOSE AND AMYLOPECTIN:

A
  • Mixture
  • Converts starch into glucose
153
Q

In the sugar industry, β-AMYLASE AND POLLULANASE:

A
  • Used to produce maltose syrup
154
Q

In the beverage industry, enzymes are used for:

A

➢ Clarification of juice
➢ Decreases the processing capacity
➢ Enhances color, flavor and texture
➢ Increase juice production, volume and color extraction
➢ Ripening

155
Q

In the beverage industry, PECTINASE:

A
  • Breaks down pectin and methanol – which is hazardous in high amounts
  • Prevents pectin from forming haze to get clear solution
  • Used for extraction of color and juice from fresh fruit
  • Increase yield
156
Q

In the beverage industry, β-GLUCANASE:

A
  • Improves clarification and filtration
  • Reduces maturation duration
157
Q

In the beverage industry, CELLULASE AND HEMICELLULASE:

A
  • Breaks down the cell wall of tea leaves and coffee cherry
  • Provide excellent fermentation process
  • Remove biopolymer and enhance the appearance of coffee and tea.
158
Q

Responsible for the browning reactions of cut fruits.

A

Phenolase

159
Q

Important in juice clarification.

A

Pectinase

160
Q

Used as meat tenderizer, partially hydrolyzes collagen and elastin.

A

Proteinase

161
Q

An endoenzyme, cleaves glycosidic bonds inside the starch molecule, decreasing its viscosity.

A

Alpha-amylase

162
Q

Is a saccharifying enzyme, increasing sweetness by cleaving glycosidic bonds outside the starch molecule.

A

Beta-amylase

163
Q

Used for bleaching flour; may destroy carotenol and vitamins; and results to off odor and off flavor in soy products.

A

Lipoxygenase

164
Q

Catalyze oxidation of glucose preventing maillard browning.

A

Glucose oxidase

165
Q

Converts sucrose to fructose and glucose; prevents crystallization of sugar in jams.

A

Invertase

166
Q

Converts glucose to fructose, important in producing high fructose syrup.

A

Glucose isomerase

FOOD TECHNOLOGY (9 decks)

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