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Samenvatting - Practicum: biotechnologie en biochemie, Michaelis Menten (J000496A)
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Practicum Michaëlis-MentenEnzymen
Substraat bindt op actieve plaats v. enyzm katalyseert
reactie evenwicht wordt sneller bereikt
Enzym komt los v. product enzym opnieuw omgezet nr.
beginproduct (D = A)
o Reactie begint opnieuw
Katalysator
Verhoogt snelheid chemische reactie
o Verlaagt activeringsenergie
o Geen invloed op ligging evenwicht
Komt onveranderd uit reactie
Grafiek
o Binden met enzym transitietoestand (hoger in E) gaat
over naar producten
o Enzym: verlagen E bij transitietoestand reactie gaat sneller
o Ligging evenwicht blijft gelijk
E en S binden in evenwichtsreactie tot ES complex
o Dissociatie v. complex met aflopende reactie nr. enzym en product
Voor steady state
o Concentratie complex stijgt (enzym-substraat-
complex)
o Concentratie enzym en substraat dalen
o Steady state: concentratie ES constant
Enzymkinetiek
Ontdekking: Brown
o Invertase: zorgt voor hydrolyse sucrose
o Initiële reactiesnelheid v verandert met substraatconcentratie [S]
2 verschillende verlopen vd. grafiek
o Lage substraat conc.: 1ste orde kinetiek
Recht evenredig verband tss. reactiesnelheid en conc. v. substraat
K = cte
v = k [S]1
o Hoge substraat conc.: 0de orde kinetiek
V bereikt plateau
V = max. bij plateau
V onafhankelijk v. substraatconc. want plateau blijft gelijk
v = k [S]0
Orthogonale hyperbool
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