2018
DOI: 10.15578/squalen.v13i1.319
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Antioxidant and Ace Inhibitor Potential of Stripe Trevally Fish (Selaroides leptolepis) Hydrolysate

Abstract: This study aimed to investigate the potency of fish protein hydrolysates (FPH) of stripe trevally fish (Selaroides leptolepis) as antioxidant and ACE inhibitor. The FPH was produced through enzymatically hydrolysis using protease produced by Bacillus licheniformis, a collection of Research and Development Center for Marine and Fisheries Product Processing and Biotechnology (RDCMFPPB). The FPH was fractionated using ultrafiltration membranes with molecular weight cut off (MWCO) of 10, 5 and 3 kDa. The hydrolysi… Show more

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Cited by 5 publications
(4 citation statements)
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References 33 publications
(31 reference statements)
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“…Yields of crude collagen, dialyzed collagen and collagen hydrolysates extracted from the body wall of golden sea cucumber* * Analyzed using one-way ANOVA a-b Different letters show significant differences in the same column (p < 0.05) 1) percentage of fresh sea cucumber 2) percentage of crude collagen 3) percentage of dialyzed collagen to one (or more) of these reasons: the decrease of enzyme activity to hydrolyze substrate (collagen hydrolysate), the reduction in the amount of accessible peptide bonds as the substrate to be digested or inhibition of the hydrolyzed product to the remaining substrate (Guérard, Dufossé, De La Broise & Binet, 2001). Putalan, Munifah, Nurhayati and Chasanah (2018) reported the similar pattern that the highest DH and peptides on hydrolysis of striped trevally f ish (Selaroides leptolepis) using B. licheniformis protease was reached after six hours of hydrolysis.…”
Section: Productmentioning
confidence: 66%
“…Yields of crude collagen, dialyzed collagen and collagen hydrolysates extracted from the body wall of golden sea cucumber* * Analyzed using one-way ANOVA a-b Different letters show significant differences in the same column (p < 0.05) 1) percentage of fresh sea cucumber 2) percentage of crude collagen 3) percentage of dialyzed collagen to one (or more) of these reasons: the decrease of enzyme activity to hydrolyze substrate (collagen hydrolysate), the reduction in the amount of accessible peptide bonds as the substrate to be digested or inhibition of the hydrolyzed product to the remaining substrate (Guérard, Dufossé, De La Broise & Binet, 2001). Putalan, Munifah, Nurhayati and Chasanah (2018) reported the similar pattern that the highest DH and peptides on hydrolysis of striped trevally f ish (Selaroides leptolepis) using B. licheniformis protease was reached after six hours of hydrolysis.…”
Section: Productmentioning
confidence: 66%
“…Dalam proses hidrolisisnya, masing-masing enzim memiliki karakteristik yang berbeda. Beberapa faktor yang harus diperhatikan dalam proses produksi HPI mengggunakan enzim antara lain suhu, waktu, jenis substrat, enzim, dan konsentrasi enzim (Putalan, Munifah, Nurhayati, & Chasanah, 2018;Utomo, Suryanigrum, & Harianto, 2014). Faktor-faktor tersebut akan berpengaruh terhadap kecepatan dan produk HPI yang dihasilkan.…”
Section: Pendahuluanunclassified
“…Penelitian lain produksi HPI dari ikan selar (Selaroides leptolepis) menggunakan enzim protease yang diproduksi oleh Bacillus sp. koleksi BBRPPBKP menunjukan derajat hidrolisis optimum pada produksi selama 6 jam (Putalan et al, 2018). Selanjutnya, produksi HPI kuniran pada skala 30 kg ikan/60 L pelarut selama 6 jam menggunakan jumlah protease 20.000 U/kg bahan baku ikan masih menyisakan residu dengan kadar protein yang cukup tinggi (Martosuyono, Fawzya, Patantis, & Sugiyono, 2019).…”
Section: Pendahuluanunclassified
“…Toopcham et al (2017) mendapatkan peptida dari tilapia dapat menghambat kerja enzim ACE 89,3%. Putalan et al (2018) menghidrolisis ikan selar menggunakan enzim protease koleksi BBRP2BKP menunjukkan hidrolisat protein ikan selar memiliki aktivitas antioksidan dan inhibitor ACE. Tujuan penelitian ini adalah mendapatkan fraksi yang memiliki aktivitas antioksidan dan inhibitor ACE dari hidrolisat protein ikan selar.…”
Section: Kadar Peptida (Church Et Al 1983)unclassified