biological molecules Flashcards

1
Q

carbohydrates contain three kinds of atoms which are

A

carbon
hydrogen
oxygen

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2
Q

what are the simplest kinds of carbohydrates

A

monosaccharide, ex.glucose

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3
Q

what is disaccharide

A

two molecules of monosaccharide joined together, ex.sucrose and maltose

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4
Q

what is polysaccharide

A

when many simple sugars join together

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5
Q

carbohydrates has a chain of?

A

glucose

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6
Q

lipids has a chain of?

A

fatty acids

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7
Q

protein has a chain of?

A

amino acids

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8
Q

lipids contain only three kinds of atoms, which are?

A

carbon
hydrogen
oxygen

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9
Q

what is a fat molecule made of

A

four smaller molecules joined together, one of these is glycerol attached to three long molecules called fatty acids

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10
Q

protein molecules contain?

A

carbon
hydrogen
oxygen
nitrogen
small amounts of sulfur

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11
Q

what is a catalyst

A

substance that increases rate of chemical reaction and doesn’t change

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12
Q

what is an enzyme

A

protein that functions as biological catalyst

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13
Q

what is the lock and key mechanism

A

the substrate molecule fits into the active site of the enzyme in a key-lock mechanism
the enzyme is the lock and the substrate is the key
after the end of the reaction the enzyme is not used up

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14
Q

properties of enzymes

A

1.all enzymes are proteins
2.lower activation energy of metabolic reaction
3.enzymes work best at certain temperature. usually 37
4.enzymes work best at a specific ph
5.they are catalysts
6.enzymes are specific

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15
Q

how does temperature affect enzyme activity

A

rate of reaction increases as temperature increases, as there is more kinetic energy so more collisions, after reaching optimum temperature enzyme becomes denatured, active site changes

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16
Q

how does pH affect enzyme activity

A

at optimum ph shape of enzyme active site fits exactly into substrate
below or above ph the shape of active site changes

17
Q

effect of substrate concentration on enzyme activity

A

as the substrate concentration increases the rate of reaction increases, due to more collisions between active site of the enzyme and substrate molecules

18
Q

what are inhibitors

A

substances that reduce the rate of enzyme catalyzed reaction

19
Q

what is competitive inhibitors

A

molecules with similar shape to the substrate, they fit into the active site stopping the substrate from entering

20
Q

what is non competitive inhibitors

A

molecules of different shape than the substrate, they attach to other parts of the enzyme, which changes the shape of the whole enzyme

21
Q

what are immobilized enzymes

A

enzymes extracted from cells or tissues and used for industrial or medical purposes

22
Q

uses of immobilized enzymes

A

1.production of lactose free milk
-some people are lactose intolerant, as they don’t have lactase enzyme which breaks down lactose into glucose and galactose, immobilized lactase is used to produce lactose free milk and is inexpensive
2.conversion of sucrose into glucose and fructose
-invertase is used commercially to break down sucrose to produce a mixture of glucose and fructose called invert syrup, invert syrup is used for sweetening products
3.testing for glucose in blood and urine
-test strips for blood or urine glucose level use two immobilized enzymes, the first one is glucose oxidase which catalayses the oxidation of glucose to gluconic acid and hydrogen peroxide, hydrogen peroxide oxidises a colorless organic substance (XH2) to it’s colored form (X). The second reaction is catalysed by immobilised peroxidase enzyme

23
Q

advantages of immobilised enzymes over dissolved enzymes

A

1.enzymes are more stable at high temperatures and are less likely to denature
2.more resistant to changes in pH
3.less likely to be broken down by organic solvents