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Characteristics of cured egg yolk cookies subtituted with skim milk powder during storage Nurliyani Nurliyani; Jamhari Jamhari; Widodo Widodo; Citravia Agustin
Jurnal Ilmu-Ilmu Peternakan (Indonesian Journal of Animal Science) Vol 32, No 1 (2022): April 2022
Publisher : Faculty of Animal Science, Universitas Brawijaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.21776/ub.jiip.2022.032.01.03

Abstract

Cured egg yolk cookies is one of the processed egg products containing egg yolk which has been curing with salt and sugar. The purpose of this study was to evaluation of physical, chemical, microbiological and sensory quality of cured egg yolk cookies with various levels of skim milk powder substitution during storage at room temperature. This study consisted of the treatment of cured egg yolk substitution with skim milk powder (0; 20; 40%) and storage treatment (0; 3; 6; 9 weeks). Each treatment was replicated three times. The data of cookie quality were statistically analyzed using ANOVA. The results showed that cured egg yolk cookies with various  skim milk powder substitution have similar physical and chemical characteristics, but substituted cookies had a lower fat content (p<0.05). There were no changes in the moisture content of cookies during 9 weeks of storage. Skim milk powder substitution could increase the peroxide number, but there was no change in the peroxide number during 3 to 9 weeks of storage.  The texture of cured egg yolk cookies with 40% skim milk substitution was harder (p<0.05) than the 20% skim milk substitution, whereas there was no change in the texture value of cured egg yolk cookies before and after being stored for 9 weeks. There was no significant deferences in the sensory quality of cookies between unsubstituted and 40% skim milk powder substitution. In conclusion, skim milk powder substitution did not change the physical, chemical, and sensory characteristics, but could reduce fat content, increase the peroxide number and the hardness of cookies. During 9 weeks of storage, cured egg yolk cookies are still acceptable microbiologically.
Mengidentifikasi Peptida Bioaktif Angiotensin Converting Enzyme-inhibitor (ACEi) dari Kasein β Susu Kambing dengan Polimorfismenya Melalui Teknik In Silico Hermawan Setyo Widodo; Tridjoko Wisnu Murti; Ali Agus; Widodo Widodo
Jurnal Aplikasi Teknologi Pangan Vol 7, No 4 (2018): November 2018
Publisher : Faculty of Animal and Agricultural Sciences, Diponegoro University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (633.952 KB) | DOI: 10.17728/jatp.3008

Abstract

Susu kambing memiliki komponen protein salah satunya protein β dan secara umum terjadi polimorfisme pada level protein. Perubahan urutan asam amino akibat polimorfisme memungkinkan adanya potensi dihasilkannya peptida bioaktif penghambat enzim pengubah angiotensin (ACEi). Penelitian ini bertujuan untuk menyaring peptida bioaktif yang berpotensi sebagai ACEi dari kasein β kambing beserta polimorfismenya. Penelitian ini dilakukan dengan teknik in silico terhadap sekuen kasein β kambing serta struktur tiga dimensi human testicular ACE. Langkah yang dilakukan dalam penelitian ini meliputi simulasi pemotongan peptida dengan enzim pencernaan (pepsin, tripsin dan kimotripsin), peninjauan karakteristik peptida lalu simulasi docking ligan-reseptor. Tampilan parameter Lipinski’s Rule of Five (Ro5), bioaktivitas dan energi afinitas dipertimbangkan untuk memilih peptida bioaktif. Hasil yang didapat menunjukkan bahwa ditemukan peptida bioaktif yakni INK (Ile-Asp-Lys) yang memiliki kemampuan hampir setara dengan lisinopril (afinitas energi -8,2kkal/mol vs. -8,3kkal/mol). Peptida INK dapat ditemukan dari hasil hidrolisis dari alel A, C, D dan E, sehingga polimorfisme tidak menyebabkan perbedaan produksi peptida bioaktif. Kesimpulan yang dapat diambil yakni kasein β susu kambing jika dicerna dengan enzim pencernaan dapat menghasilkan peptida bioaktif ACEi yakni INK.Identification of Angiotensin Converting Enzyme-inhibitor (ACEi) Bioactive Peptide from Goat Milk β-Casein with It's Polymorphism by In Silico TechniqueAbstractPolymorphism eventually may be occurred at the protein level. Changes in the amino acid sequence due to polymorphism may exhibit a potential action to generate of the angiotensin-converting enzyme inhibitors (ACEi) bioactive peptide. This study is aimed to assess bioactive peptides that have a great potent value as ACEi from goat β casein along with its polymorphism. The research was done by in silico technique on goat β-casein sequence and three-dimensional structure human testicular ACE. Peptide-cutting simulations with digestive enzymes (pepsin, trypsin and chymotrypsin), peptide properties review, then ligand-receptor docking simulations was applied in this research. Appearance of Lipinski's Rule of Five (Ro5), bioactivity and affinity energy were considered for selecting bioactive peptides. The results show that bioactive peptide found as INK (Ile-Asp-Lys) which had similar ability as lisinopril (energy affinity –8.2kcal/mol vs. –8.3kcal/mol). The INK peptides could be found from the hydrolysis resulted in alleles A, C, D and E, therefore polymorphism did not affect the differences of production of bioactive peptides. A conclusion, processed goat milk β casein with digestive enzymes could produce ACEi of INK as bioactive peptide.