Immobilization Flashcards

1
Q

The restriction of enzyme mobility in a fixed space

A

Enzyme immobilization

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2
Q

Immobilization of enzymes provides important advantages, such as enzyme _____ and ____ of enzyme recovery and purification processes, and may provide a better environment for enzyme activity.

A

reutilization, elimination

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3
Q

usually improved, and effluent handling problems are minimized by immobilization.

A

Product purity

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4
Q

physical enclosure of enzymes in a small space

A

Entrapment

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5
Q

two major methods of entrapment

A

Matrix entrapment and membrane entrapment

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6
Q

used for enzyme immobilization are usually polymeric materials such as Ca-alginate, agar, k-carrageenin, polyacrylamide, and collagen

A

Matrices

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7
Q

some solid matrices such as activated carbon, ___, and ____ earth can be also used for this purpose.

A

porous cerami ,diatomaceous

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8
Q

can be a particle, a membrane, or a fiber

A

Matrix

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9
Q

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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10
Q

___ and ____ attachment may be used in combination in some cases.

A

Entrapment, surface

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11
Q

common materials used for membranes in enzyme entrapment

A

Nylon, cellulose, polysulfone, and polyacrylate

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12
Q

used to retain high molecular weight compound

A

semipermeable membrane

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13
Q

membrane can be polymeric or an enriched interfacial phase formed around a micro drop

A

microencapsulation

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14
Q

involves forming microscopic hollow spheres that contain the enzyme solution, enclosed within a porous membrane

A

Microencapsulation

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15
Q

can be minimized by reducing the molecular weight cutoff of membranes or the pore size of solid matrices

A

Enzyme leakage

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16
Q

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

A

Diffusional limitations

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17
Q

usually less significant in microcapsules as compared to gel beads.

A

Diffusion barrier

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18
Q

two major types of surface immobilization of enzymes

A

adsorption and covalent binding

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19
Q

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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20
Q

The active site of the adsorbed enzyme is usually ____, and nearly full activity is retained upon adsorption.

A

unaffected

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21
Q

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

A

Desorption of enzymes

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22
Q

stabilized by cross-linking with glutaraldehyde. Glutaraldehyde treatment can denature some proteins.

A

Adsorption

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23
Q

Support materials used for enzyme adsorption

A

Inorganic - alumina, silica, porous glass, ceramics, diatomaceous earth, clay, bentonite.
Organic - cellulose (CMC, DEAE-cellulose), starch, activated carbon, and ion exchange resins, such as Amberlite, Sephadex, and Dowex

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24
Q

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

A

Covalent binding

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25
Q

bind to support material via certain functional groups, such as amino, carboxyl, hydroxyl, and sulfhydryl groups.

A

Enzyme molecules

26
Q

flooding the enzyme solution with a competitive inhibitor prior to covalent binding.

A

Blocking the active site

27
Q

molecules with agents such as glutaraldehyde can help in enzyme immobilization

A

Cross-linking enzyme

28
Q

___ and ___ of an enzyme from an organism require disruption of cells, removal of cell debris and nucleic acids

A

Separation, purification

29
Q

varies depending on whether the enzyme is intracellular or extracellular

A

Orocess scheme

30
Q

can be regulated and fermentation conditions can be optimized for overproduction of the enzyme

A

Enzyme production

31
Q

produced by using overproducing strains of Bacillus, Aspergillus, Rhizopus, and Mucor

A

Proteases

32
Q

produced by Aspergillus niger; lactases are produced by yeast and Aspergillus

A

Pectinases

33
Q

produced by certain strains of yeast and fungi

A

Lipases

34
Q

produced by Flavobacterium arborescens or Bacillus coagulans

A

Glucose isomerase

35
Q

are commonly used methods to separate cells from the media after the cultivation step

A

Filtration or centrifugation

36
Q

may be released by increasing the permeability of cell membrane

A

Intracellular enzymes

37
Q

hydrolyze proteins into smaller peptide units and constitute a large and industrially important group of enzymes

A

Proteases

38
Q

Proteases constitute about __ of the total enzyme market

A

60%

39
Q

Most of the industrial proteases

A

Endo proteases

40
Q

are used in food processing (cheese making, baking, meat tenderization, brewing), in detergents for hydrolysis of protein stains, and in tanning and medical treatment for wounds

A

Proteases

41
Q

produced mainly by A. niger. used in fruit juice processing and wine making to increase juice yield, reduce viscosity, and clear the juice

A

Pectinase

42
Q

are used to hydrolyze oils for soap manufacture, in wastewater treatment, in the cheese and butter industry to impart flavor, and in lipase-containing detergents

A

Lipases

43
Q

used for the hydrolysis of starch and are produced by many different organisms including A. niger and B. subtilis

A

Amylases

44
Q

breaks a -1,4 glycosidic bonds randomly on the amylose chain and solubilizes amylose. And is known as the starch liquefying enzyme.

A

A-amylase

45
Q

hydrolyzes a -1,4 glycosidic bonds on the nonreducing ends of amylose and produces maltose residues. And is known as a saccharifying enzyme.

A

B-amylase

46
Q

hydrolyzed to glucose by beta-glucosidase

A

Cellulases

47
Q

used in cereal processing, alcohol fermentation from biomass, brewing, and waste treatment

A

Cellulases

48
Q

five-carbon sugar units and are produced by some molds, such as white rot fungi and A. niger

A

Hemicellulases

49
Q

used in the fermentation of cheese.

A

Lactases

50
Q

is used by the antibiotic industry to convert penicillin G to 6aminopenicillanic acid (6-APA), which is a precursor for semisynthetic penicillin derivatives.

A

Penicillin acylase

51
Q

low-calorie sweetener

A

NutraSweet

52
Q

coupled with Lphenylalanine to produce aspartame

A

Aspartate

53
Q

nearly 1.7 times sweeter than glucose and is used as a sweetener in softdrinks

A

Fructose

54
Q

commonly used in medicine for diagnosis, therapy, and treatment purposes

A

Enzymes

55
Q

can be used as an anti-inflammatory agent

A

Trypsin

56
Q

hydrolyzes the cell wall of gram-positive bacteria, is used as an antibacterial agent.

A

lysozyme

57
Q

used as an anti-inflammatory agent

A

Streptokinase

58
Q

dissolving and preventing blood clots

A

Urokinase

59
Q

produced by E. coli

A

Asparaginase

60
Q

used for the determination of glucose levels in blood and urine

A

Glucose oxidase

61
Q

used to treat allergic reactions against penicillin.

A

Penicillinases

62
Q

used in the dissolution of blood clots

A

Tissue plasminogen activator (TPA) and streptokinase