Enzyme

​Calculating the Rate of the Reaction of an Enzyme

​A rate means “over a set time”

•  Formula:

  • Amount of product formed / Time= rate of reaction

Ex: Lactase underwent a reaction with its substrate lactose.  25 glucose / galactose molecules were formed in 250 seconds.  What was the rate of the reaction?

 0.1 molecules produced per second

​Denaturation of enzymes:

• structural change in a protein / enzyme resulting in 

  •  breaking hydrogen bonds

• Caused by heat and pH extremes

​Application: Using Immobilized  enzymes in Industry

• enzyme attached to material  restricting movement

  •  Provides fastest rate of reaction

• Common Uses:

  • Detergent Industry (cleaning products)

  • Biotech Industry (gene cutting / splicing)

  • Food Industry (juice extraction, lactose free milk)

​The production of lactose free milk

• Enzyme:  Lactase

  •  extract lactase from yeast or bacteria 

  •  bind it to beads to immobilized it

Substrate: Lactose

•  Milk (Containing lactose) is passed over beads

• Lactose: disaccharide made of glucose + galactose

• Products:  glucose and galactose

  • Disaccharide lactose is broken into its monomers

•  Milk contains glucose and galactose (not lactose)

  • “Lactose free”

Advantages to Lactose-free products:

•  milk for people with lactose intolerance

  • after weaning mammals exhibit a decreased natural lactase production

•  reduces crystallization of ice creams

  • glucose and galactose are more soluble  

•  shortening production time of yo

  • bacteria ferment glucose and galactose more efficiently  

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​Competitive Inhibition

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​Noncompetitive Inhibition

•  Uses inhibitor molecules

  • similar to substrate

  •  competes with substrates to bind to active site of enzyme

    • inhibitor prevents substrate from binding 

• reversible

  •  inhibitors’ effects are reduced by increased substrate concentration

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Competitive inhibition on a graph=

• If more inhibitor than substrate:  Vmax is low

• Increasing substrate concentration:  increases Vmax

• Vmax can return to normal: if much higher substrate concentration than inhibitor

Non-competitive Inhibition

•  molecule binds to allosteric site

  • not similar to substrate

•  causes conformational change in active site

  • substrate can no longer bind 

•  Reversible IF inhibitor is removed