ENZYME

OLEH

YANA CAHYANA STP.,DEA.,Ph.D

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 Outline
- Introduction
- Catalytic power, specificity, &
regulation
- Kinetics of enzyme-catalysed
reaction
- Enzyme inhibition

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 Introduction
Enzymes are fundamental to biochemistry, the food
sciences and biotechnology
Much of biotechnology is concerned either with
producing or using enzymes
Applications are in a wide range of sectors -
particularly the food industry
Any practising biotechnologist, biochemist or food
scientist will work with enzymes at some point
Knowledge of the fundamentals of enzymology is
important

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 Introduction
Nama :
-ase : invertase, triosa fosfat dehidrogenase
-in : pepsin, chymotrypsin
Lisozim?

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 Introduction
Karakteristik enzim
-Katalisator reaksi
-Mengubah substrat jadi produk
-Protein
-Bekerja spesifik
-Berat molekul (BM) enzim>>>> (BM) substrat
-Mempunyai gugus dan ruang aktif
-Mempunyai bagian non protein
-Kompleks E-S merubah bentuk ruang aktif dan substrat

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 Introduction
Enzim bekerja dengan menurunkan energi aktifasi

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 Catalytic power, specificity, &
regulation
- Accelerating reaction rate as much as 1016 over
uncatalysed levels
ex urease catalyses the hydrolysis of urea :

Catalysed reaction : 3 x104/sec

Uncatalysed one : 3 x 10-10/sec
Catalytic power of urease =1014

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 Catalytic power, specificity, &
regulation

-Molecular recognition based on structural

complementarity
-Specific site on the enzyme where substrate binds and
catalysis occurrs is called the active site

-Some enzymes rely solely on their amino acid residues,

others require cofactor either metal ions (Fe2+,Fe3+, Mg2+,
Cu2+, Mg2+, Se) or organic molecules (coenzyme, ex:
vitamin).

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 Enzyme Kinetics
-Pengaruh suhu pada aktifitas enzim

-Pengaruh pH pada aktifitas enzim

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 Enzyme Kinetics
-Pengaruh konsentrasi enzim

-Pengaruh konsentrasi substrat

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 Enzyme Kinetics
-Michaelis-Menten Equation

v= kecepatan reaksi enzimatis, Vmax=kecepatan maksimum

Kmax=konstanta Michaelis-Menten, [S]=konsentrasi substrat

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 Enzyme Kinetics
Konstanta Michaelis-Menten (Km)

-Salah satu ciri enzim

-Menggambarkan afinitas enzim terhadap substrat

Km afinitas

-Km <10-6M sangat penting dalam metabolisme,

Km >10-2M dianggap kurang penting

-Kerja penghambatan enzim Nilai Km

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Konstanta Michaelis-Menten (Km)

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 Enzyme Kinetics
Transformation of Michaelis-Menten equation :
Lineweaver-burk double reciprocal plot

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 Enzyme Unite
-Aktifitas enzim= banyaknya substrat yang dirubah menjadi produk
oleh sejumlah enzim
-Aktifitas enzim dinyatakan dalam unit (U)

1 unit= jumlah enzim yg dapat mengkatalisis 1 mol substrat per

menit pada kondisi tertentu
Enzyme activity (U)
Specific activity = Amount of protein present (mg)

Cellulase 1000 U/g

-Amylase 200 U/g
Polygalacturonase 280 U/g
Glucoamylase 570 U/g
-1,3-Glucanase 1970 U/g
Protease 2000 U/g
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 Enzyme Inhibition
Many compounds can inhibit enzymes

Highly reactive chemicals can form covalent

bonds with reactive groups on the enzyme and
irreversibly inhibit the enzyme

Other molecules interact with the enzyme in

reversible ways to produce inhibition

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 Enzyme Inhibition

Reversible Irreversible
(Ikatan non kovalen) (Ikatan kovalen)

-Kompetitif
-Non kompetitif
- Kombinasi

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 Enzyme Inhibition
Penghambatan Kompetitif

-Inhibitor bersaing dengan substrat

memperebutkan ruang aktif yang
sama

Contoh:
Pemberian etanol bagi yang keracunan
metanol

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 Enzyme Inhibition
Penghambatan Non-Kompetitif
inhibitors bind to the enzyme-substrate complex and block the catalytic step

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 Enzyme Inhibition
Penghambatan Kombinasi (Campuran)

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 Enzyme Inhibition
Penghambatan Irreversible

Penicilin menghambat glycoprotein peptidase

dalam croslinking peptidoglikan untuk sintesa
dinding sel

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