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Title: | Karakteristik Protein Serisin Kokon Ulat Sutra Eri (Samia cynthia ricini) dengan Larutan Degumming NaOH 0,25 N. |
Other Titles: | Characteristic Sericin Protein Cocoon of Eri (Samia cynthia ricini) using Different NaOH Solvent Concentrations |
Authors: | Endrawati, Yuni Cahya Darmawan, Noviyan Effendy, Muhamad Jull |
Issue Date: | 2023 |
Publisher: | IPB University |
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. |
URI: | http://repository.ipb.ac.id/handle/123456789/116809 |
Appears in Collections: | UT - Technology of Cattle Products |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Cover.pdf Restricted Access | Cover | 2.24 MB | Adobe PDF | View/Open |
D34180012_Muhamad Jull Effendy.pdf Restricted Access | Fullteks | 3.04 MB | Adobe PDF | View/Open |
Lampiran.pdf Restricted Access | Lampiran | 1.08 MB | Adobe PDF | View/Open |
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