Immobilize Enzyme System Flashcards

1
Q

The restriction of enzyme mobility in a fixed space is known as ______. This provides important advantages,
such as enzyme reutilization and elimination of enzyme recovery and purification processes, and may provide a better environment for enzyme activity.

A

Enzyme Immobilization

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2
Q

Since enzymes are expensive,
this is critical for many
processes.

A

Catalyst-reuse

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3
Q

is the physical enclosure of enzymes in a small space.

A

Entrapment

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4
Q

Major methods of Entrapment

A

Matrix entrapment and Membrane entrapment

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5
Q

used for enzyme immobilization are usually
polymeric materials such as Ca-alginate, agar, k-carrageenin, polyacrylamide, and collagen. However, some solid such as activated carbon, porous ceramic, and diatomaceous earth can also be
used for this purpose.

A

Matrices

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6
Q

it can be a particle, a
membrane, or a fiber.

A

Matrix

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7
Q

is either extruded or a template is used to shape the particles from a liquid polymer-enzyme mixture.

A

Polymerized gel-containing enzyme

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8
Q

entrapment of enzymes
is possible; for example, hollow
fiber units have been used to
entrap an enzyme solution
between thin, semipermeable
membranes.

A

Membrane Entrapment

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9
Q

A special form of membrane
entrapment is _______. In this technique, microscopic
hollow spheres are farmed. The
spheres contain the enzyme
solution, while the sphere is
enclosed within a porous
membrane. The membrane can be polymeric or an enriched
interfacial phase formed around a microdrop.

A

Microencapsulation

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10
Q

can be overcome by reducing the MW cutoff of membranes or the pore size of solid matrices.

A

Enzyme Leakage

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11
Q

can be eliminated by reducing the particle size of matrices and/or capsules.

A

Diffusion Limitation

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12
Q

are due to unfavorable
microenvironmental conditions,
which are difficult to control.
However, by using different
matrices and chemical ingredients, by changing processing conditions, and by reducing particle or capsule size, more favorable microenvironmental conditions can be obtained.

A

Reduced enzyme activity and
stability

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13
Q

is usually less significant in microcapsules as compared to gel beads.

A

Diffusion Barrier

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14
Q

The two major types of
immobilizations of enzymes on the surfaces of support materials are

A

Adsorption and Covalent Binding

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15
Q

is the attachment of
enzymes on the surfaces of support particles by weak physical forces, such as van der Waals or dispersion forces

A

Adsorption

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16
Q

is a common problem, especially in the presence of strong hydrodynamic forces, since binding forces are weak.

A

desorption of enzymes

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17
Q

The _______ of the adsorbed
enzyme is usually unaffected, and nearly full activity is retained upon adsorption.

A

Active Site

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18
Q

Adsorption of enzymes may be
stabilized by cross-linking with “blank”. “Blank” treatment can denature some proteins.

A

Glutaraldehyde

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19
Q

is the retention of enzymes on support surfaces by covalent bond formation.

A

Covalent Binding

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20
Q

Enzyme molecules bind to support material via certain “blank”, such as amino, carboxyl, hydroxyl, and sulfhydryl groups.

A

functional groups

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21
Q

These functional groups must not be in the

A

Active Site

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22
Q

Functional groups on support
material are usually activated by using “blank”, such as
cyanogen bromide, carbodiimide, and glutaraldehyde.

A

Chemical Reagent

23
Q

One common trick Is to block the active site by flooding the enzyme solution with a “blank” prior to covalent binding.

A

Competitive Inhibitor

24
Q

This may cause significant changes in the active
site of enzymes, and also severe diffusion limitations may result.

A

Cross-linking

25
Two major criteria used in the selection of support material
(1) the binding capacity of the support material, which is a are function of charge density, functional groups, porosity, and hydrophobicity of the support surface, and (2) stability and retention of enzymatic activity, which is a function of functional groups on support material and microenvironmental conditions.
26
If immobilization causes some conformational changes on the enzyme, or if reactive groups on the active site of the enzyme are involve in binding, a "blank" in enzyme activity can take place upon immobilization.
Loss
27
it may be more advantageous to use "blank" with the desired enzyme activity in Immobilized form. This approach eliminates costly enzyme separation and purification steps and is therefore economically more feasible.
inactive (dead or resting) cells
28
are produced by using overproducing strains of Bacillus, Aspergillus, Rhizopus, and Mucor
Proteases
29
are produced by Aspergillus niger, lactases are produced by yeast and Aspergillus;
Pectinases
30
are produced by certain strains of yeasts and fungi;
Lipases
31
is produced by Flavobacterium arborescens or Bacillus coagulans.
Glucose Isomerace
32
If enzyme release is not complete, then "blank" may be essential.
Cell Disruption
33
Intracellular enzymes may be released by increasing the permeability of cell membrane. Certain salts such as "blank" and other chemicals such as "blank" and pH shift may be used for this purpose.
CaCl₂ dimethylsulfoxide (DMSO)
34
hydrolyze proteins into smaller peptide units and constitute a large and industrially important group of enzymes:
Proteases
35
Most of the industrial proteases are
Endoproteases
36
are used in food processing, such as cheese making (rennet), baking, meat tenderization (papain, trypsin), and brewing (trypsin, pepsin); in detergents for the hydrolysis of protein stains (subtilisin Carlsberg); and in tanning and the medical treatment of wounds.
Proteases
37
are used in fruit juice processing and wine making to increase juice yield, reduce viscosity, and clear the juice.
Pectinases
38
may be used to hydrolyze oils for soap manufacture and to hydrolyze the lipid-fat compounds present in waste-water streams.
Lipases
39
-1.6 glycosidic linkages in the amylopectin fraction of starch are hydrolyzed by "glucoamylase", which is also known as a
saccharifying enzyme.
40
A -amylase breaks a -1,4 glycosidic bonds randomly on the amylose chain and solubilizes amylose. For this reason, a-amylase is known as the
starch liquefying enzyme
41
are used in cereal processing, alcohol fermentation from biomass, brewing, and waste treatment.
Cellulases
42
are used in combination with other enzymes in baking doughs, brewing mashes, alcohol fermentation from biomass, and waste treatment.
Hemicellulases
43
are used in the fermentation of cheese. And are used to hydrolyze lactose in when to glucose and galactose
Lactases
44
is used by the antibiotic industry to convert penicillin G to 6-aminopenicillanic acid (6-APA), which is a precursor for semisynthetic penicillin derivatives.
Penicillin Acylases
45
The conversion of glucose to fructose by immobilized "blank" is an important industrial process. Fructose is nearly 1.7 times sweeter than glucose and is used as a sweetener in softdrinks.
Glucose Isomerace
46
can be used as an anti-inflammatory agent, lysozyme which hydrolyzes the cell wall of gram-positive bacteria, is used as an antibacterial agent.
Trypsin
47
is used as an anti-inflammatory agent. aside from Trypsin
Streptokinase
48
is used in dissolving and preventing blood clots.
Urokinase
49
is used as an anticancer agent.
Asparaginase
50
is used for the determination of glucose levels in blood and urine.
Glucose Oxidase
51
hydrolyze penicillin and are used to treat allergic reactions against penicillin.
Penicillinases
52
are used in the dissolution of blood clots (particularly following a heart attack or stroke).
Tissue plasminogen activator (TPA) and streptokinase
53