Penentuan Struktur Tiga Dimensi dan Profil Hasil Hidrolisis Protein Alergen Arginin Kinase Secara in silico

Abstract

ABSTRAK: Alergi pangan ialah suatu reaksi hipersensitivitas melalui mekanisme imunologis setelah terpapar alergen dari suatu bahan pangan. Arginin kinase dengan kode alergen (Pen m 2) merupakan alergen yang terdapat di bahan pangan udang windu ( Penaeus monodon ) dan dapat memicu terjadinya alergi. Tujuan dari penelitian ini untuk mendapatkan struktur tiga dimensi dan mendapatkan profil hidrolisat arginin kinase secara in silico . Metode penelitian identitas karakteristik fisikokimia arginine kinase family, molekul, nilai grand average of hidropathicity (GRAVY) indeks kestabilan. ialah penentuan struktur tiga dimensi. ialah memprediksi profil hasil hidrolisis protein alergen arginin kinase secara enzimatis (pepsin, dan kimotripsin) dan non-enzimatis (asam format). Hasil penelitian ini menjelaskan bahwa Pen m 2 merupakan family ATP:guanido phosphotransferase dengan pola kinase fosfagen. Struktur tiga dimensi Arginin kinase (Pen m 2) memiliki hasil identitas sekuens 96,91% dan nilai Ramachandran favoured ialah 97,18%. Hidrolisis arginin kinase menggunakan enzim pepsin, kimotripsin dan tripsin menghasilkan peptida terpanjang 11 asam amino (berat molekul 1210 Da), sehingga menunjukkan penurunan alergenisitas arginin kinase (Pen m 2). Hidrolisis menggunakan asam format menghasilkan peptida terpanjang ialah 69 asam amino (berat molekul 7590 Da) yang masih berpotensi alergenik Kata kunci: arginin kinase, in silico , pemotongan peptida, SWISS-MODEL, udang ABSTRACT: Food allergy is a hypersensitivity reaction through an immunological mechanism after exposure to an allergen from a food ingredient. Arginine kinase with an allergen code (Pen m 2) is an allergen found in tiger prawns (Penaeus monodon) and can trigger allergies. This study aimed to obtain a three-dimensional structure and an in silico profile of arginine kinase hydrolyzate. The research method in the first stage is the search for identity and physicochemical characteristics of arginine kinase in the form of family, molecular weight, theoretical pI value, and grand average of hydropathicity (GRAVY) and stability index. The second stage is the determination of the three-dimensional structure. The third step is to predict the profile of the hydrolysis of the allergen arginine kinase protein enzymatically (pepsin, trypsin and chymotrypsin) and non-enzymatically (formic acid). The results of this study explain that Pen m 2 is a family of ATP:guanido phosphotransferases with a phosphagen kinase pattern. The three-dimensional structure of Arginine kinase (Pen m 2) has a sequence identity result of 96.91%, and the Ramachandran favoured value is 97.18%. Hydrolysis of arginine kinase using the enzymes pepsin, chymotrypsin and trypsin resulted in the longest peptide of 11 amino acids (molecular weight 1210 Da), thus indicating a decrease in the allergenicity of arginine kinase (Pen m 2). Hydrolysis using formic acid resulted in the most extended peptide being 69 amino acids (molecular weight 7590 Da) which was still potentially allergenic.