Update Artikelilmiah: 12304

NURLISA CHUMAIROH

NIM

Judul Artikel

Abstrak (Bhs. Indonesia)

Kinetika reaksi enzim merupakan cabang ilmu kimia yang mengkaji laju dari reaksi enzim. Reaksi enzim dapat dihambat oleh inhibitor kompetitif yang berkompetisi dengan substrat untuk menempati sisi aktif enzim. Pada penelitian ini, dikaji model kinetika reaksi enzim dengan inhibitor kompetitif yang dapat disederhanakan menjadi persamaan laju reaksi. Perbandingan persamaan laju reaksi tanpa inhibitor dan persamaan laju reaksi dengan inhibitor kompetitif dilakukan untuk mengetahui pengaruh inhibitor kompetitif pada reaksi enzim. Berdasarkan persamaan laju reaksi, diperoleh bahwa  konstanta Michelis-Menten pada reaksi enzim dengan inhibitor kompetitif lebih besar dibanding reaksi enzim tanpa inhibitor. Hal ini menyebabkan laju reaksi pada reaksi enzim dengan inhibitor kompetitif lebih kecil dibanding reaksi enzim tanpa inhibitor, tetapi pada saat konsentrasi substrat sangat besar sama-sama akan mendekati laju reaksi maksimum. Persamaan Lineweaver-Burk pada reaksi enzim dengan inhibitor kompetitif digunakan untuk menentukan konstanta Michelis-Menten dan laju reaksi maksimum dengan tepat. Aplikasi persamaan Lineweaver-Burk pada reaksi enzim xantin oksidase tanpa inhibitor dan reaksi enzim xantin oksidase dengan inhibitor ekstrak daun sidaguri menghasilkan konstanta Michelis-Menten untuk reaksi enzim xantin oksidase dengan inhibitor ekstrak daun sidaguri lebih besar dibanding konstanta Michelis-Menten untuk reaksi enzim xantin oksidase tanpa inhibitor. Sementara itu, laju reaksi maksimum sama.

Abtrak (Bhs. Inggris)

Kinetics of enzymatic reaction is the study of chemistry that examines the rates of enzymatic reaction. Enzymatic reaction can be inhibited by competitive inhibitor which competes with the substrate to occupy the active site of an enzyme. In this research, the model of enzyme kinetics with competitive inhibitor which can be simplified to reaction rate equation is studied. The comparison of reaction rate equation without inhibitor and reaction rate equation with competitive inhibitor is done to define the influence of competitive inhibitor on enzymatic reaction. Based on the reaction rate equation, it is obtained that Michelis-Menten constant on enzymatic reaction with competitive inhibitor is bigger than enzymatic reaction without inhibitor. It causes the reaction rate on enzymatic reaction with competitive inhibitor is smaller than enzymatic reaction without inhibitor, but at higher substrate concentrations, they both will approach maximum reaction rate. Lineweaver-Burk equation on the enzymatic reaction with competitive inhibitor is used to determine Michelis-Menten constant and maximum reaction rate precisely. The application of Lineweaver-Burk equation on xanthine oxidase enzymatic reaction without inhibitor and xanthine oxidase enzymatic reaction with sidaguri leaf extract inhibitor obtains Michelis-Menten constant for xanthine oxidase enzymatic reaction with sidaguri leaf extract inhibitor bigger than Michelis-Menten constant for xanthine oxidase enzymatic reaction without inhibitor. Meanwhile, the maximum reaction rates are equal.

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