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Biochemical Engineering > Lecture 2 > Flashcards

Lecture 2 Flashcards

1
Q

Oxidation – reduction reactions

A

Oxidoreductase

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2
Q

Transference of an atom or group
between two molecules

A

Transferases

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3
Q

Hydrolysis reactions

A

Hydrolases

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4
Q

Removal of a group from a substrate (not by hydrolysis

A

Lyases

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5
Q

Isomerisation reactions

A

Isomerases

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6
Q

joining of two molecules

A

Ligases

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7
Q

Assumptions of Michaelis Menten equation

A

[S]0»»[E]0
The concentration of the intermediate [ES] attains a steady state value shortly after the start of the reaction

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8
Q

Michaelis Menton équation

A

Vm [S]/ Km + [S]

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9
Q

Disadvantage of Lineweaver Burke plot

A

Long extrapolation needed to determine Km

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10
Q

Restriction of enzyme mobility in a fixed spot

A

Enzyme immobilisation

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11
Q

Advantages of enzyme immobilisation

A

Catalyst reuse
Easier reactor operation
Easier product separation
Wider choice of reactor

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12
Q

Disadvantages of enzyme immobilisation

A

Loss or reduction in activity
Diffusional limitation
Additional cost

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13
Q

Factors for choosing supports

A
  • Physical resistance to compression
  • Hydrophilicity
  • Inertness toward enzymes
  • Biocompatibility
  • Resistance to microbial attack
  • Availablity at low cost
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14
Q

Physical enclosure of enzymes in a small space

A

Entrapment

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15
Q

Matrices used are polymetric materials

A

Matrix entrapment

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16
Q

Microcapsulation or trapped between thin, semi-permeable membranes

A

Membrane entrapment

17
Q

Advantages of entrapment

A
  • enzyme is retained
  • no chemical modification/relatively stable forms
  • easy handling and reusage
18
Q

Disadvantages of entrapment

A
  • Enzymes could leak into the solution
  • Substrate need to diffuse in to access enzyme and product need to diffuse out
  • If the conditions used in the polymerisation reaction are severe, it could lead to loss of enzyme activity
19
Q
  • Van der Waals
  • -Hydrophobic-hydrophilic interactions
  • Carriers: silica, carbon nanotubes, cellulose etc.
  • Easy desorbed, simple and cheap, enzyme activity unaffected
A

Physical adsorption

20
Q
  • ionic bonds
  • similar to physical adsorption
  • carriers: polysaccharides and synthetic polymers with ion-exchange centers
A

ionic binding

21
Q
  • retention of the enzymes by covalent bonds
  • carriers: polymers contain amino, carboxyl, sulfhydryl, hydroxyl, or phenolic groups
A

covalent binding

22
Q

Is to cross link enzyme molecules with each other using agent such as glutaraldehyde
Features: similar to covalent bindings
Several methods are combined

A

Cross linking

23
Q

stability of enzymes

A

enzyme half life

24
Q

half life equation for first order reaction

A

t1/2 = ln 2/k

Biochemical Engineering (6 decks)

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