Karakteristik Protein Serisin Kokon Ulat Sutra Eri (Samia cynthia ricini) dengan Larutan Degumming NaOH 0,25 N.

Abstract

Serisin merupakan protein globular penyusun kokon ulat sutra yang memiliki beragam manfaat di bidang pangan, kosmetik, farmasi, dan biomedis. Pada penelitian sebelumnya, rendemen serisin yang diperoleh menggunakan larutan degumming NaOH 0,1 N belum optimal. Penelitian ini bertujuan menganalisis rendemen protein, bobot molekul, dan susunan asam amino protein serisin kokon ulat sutra Eri dengan larutan degumming NaOH 0,25 N. Hasil ekstraksi protein serisin dengan larutan degumming NaOH 0,25 N menghasilkan rendemen serisin sebesar 23,6±4,1%. Hasil tersebut lebih baik dibandingkan bila menggunakan larutan degumming NaOH 0,1 N (4,8±1,5%). Bobot molekul protein serisin hasil isolasi memiliki rentang bobot molekul protein 15,68-45,70 kDa yang sesuai dengan kisaran bobot molekul serisin dari literatur. Hasil analisis HPLC menunjukan bahwa komponen asam amino utama protein serisin adalah alanina, glisina, dan tirosina.

Sericin is a globular protein forming silkworm coccon that have various function in foods, cosmetics, pharmaceuticals, and biomedical industry. Previous research have used 0.1 N NaOH degumming solvent and considered not optimal in producing yields. This research purpose to analyze the protein yield, molecular weight, and amino acid composition of the Eri silkworm cocoon sericin protein using 0.25 N NaOH degumming solvent. The results of protein sericin extraction with 0,25 N NaOH degumming solvent resulted sericin yield of 23.6%±4,1. These result is better than using NaOH 0.1 N degumming solvent (4,80%±1,51). The molecular weight of isolation sericin protein is 15.68-45.70 kDa which corresponds to the range of molecular weights from the literature. The result of the HPLC analysis showed that the main amino acid components of the sericin protein is alanine, glisine, and tyrosine.