| dc.contributor.advisor | Endrawati, Yuni Cahya | |
| dc.contributor.advisor | Agustina, Fitria | |
| dc.contributor.author | Nur, Fitri Febrianti | |
| dc.date.accessioned | 2022-03-06T23:50:21Z | |
| dc.date.available | 2022-03-06T23:50:21Z | |
| dc.date.issued | 2022 | |
| dc.identifier.uri | http://repository.ipb.ac.id/handle/123456789/111288 | |
| dc.description.abstract | Protein serisin merupakan perekat antar serat (fibril). Protein serisin diekstraksi dari limbah air degumming serat sutra. Serisin Samia cynthia ricini didapatkan dengan melakukan degumming menggunakan NaOH 0,033N dengan kombinasi suhu dan waktu 113 oC selama 34 menit. Hasil crude protein serisin kemudian dipurifikasi dengan netralisasi menggunakan HCL serta presipitasi etanol.
Hasil purifikasi dikarakterisasi berat molekulnya menggunakan sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) dan didapatkan hasil berat molekul serisin sebesar 7,08 kDa. Asam amino serisin S. ricini dikarakterisasi menggunakan high performance liquid chromatography (HPLC) dan dihasilkan asam amino tertinggi pada glisina (15,35%). Aktivitas dalam penghambatan DPPH
diketahui sebesar 66,86% dengan kapasitas antioksidan 8,03 mg VCE mL-1. Sifat antibakteri dimiliki serisin S. ricini terhadap bakteri S. aureus dengan zona hambat 6,74 mm dan persentase penurunan kekeruhan 80.04%. | id |
| dc.description.abstract | Sericin is a protein that acts as an adhesive joining two fibroin filaments. Sericin protein was extracted from silk wastewater. Silk wastewater was produced from degumming of cocoon Samia cynthia ricini with NaOH 0,033N and a combination of temperature and time 113 oC for 34 minutes. Crude sericin protein was purified with neutralization of HCL and ethanol precipitation. The molecular weight of purified protein was investigated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and the results of S. ricinisericin molecular weight is 7,08 kDa. The amino acid of S. ricini sericin was investigated by high performance liquid chromatography (HPLC) that result in highest component is glycine (15,35%). Sericin S. ricini has 66,86% antioxidant activity with 8,03 mg VCE mL-1 antioxidant capacity. Antibacterial attribute of sericin S. ricini inhibit toward S. aureus bacteria with 6,74 mm inhibition zone and 80,04% in turbidity decrease percentage. | id |
| dc.language.iso | id | id |
| dc.publisher | IPB University | id |
| dc.title | Purifikasi dan Karakterisasi Protein Serisin Kokon Ulat Sutra Eri (Samia cynthia ricini) | id |
| dc.title.alternative | Purification and Characterization Sericin Protein Cocoon of Eri (Samia cynthia ricini) silkworm | id |
| dc.type | Undergraduate Thesis | id |
| dc.subject.keyword | purification | id |
| dc.subject.keyword | Samia cynthia ricini | id |
| dc.subject.keyword | sericin | id |
| dc.subject.keyword | SDS-PAGE | id |
| dc.subject.keyword | HPLC | id |
