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      Produksi Kontinu Peptida Bioaktif dari Konsentrat Protein Koro Benguk dengan Enzim Alkalase dalam Reaktor Membran Enzimatis

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      Date
      2023
      Author
      Fadli, Ahmad
      Sitanggang, Azis Boing
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      Abstract
      Peptida bioaktif yang berasal dari sumber protein dapat dijadikan sebagai sumber untuk menghasilkan pangan fungsional yang memiliki efek terhadap kesehatan. Salah satu protein nabati yang memiliki potensi sebagai sumber peptida bioaktif adalah koro benguk. Penelitian ini bertujuan memproduksi peptida bioaktif koro benguk secara kontinu dengan menggunakan reaktor membran enzimatis dengan kondisi optimum. Peptida bioaktif yang memiliki aktivitas antioksidan dapat dihasilkan dengan menghidrolisis sumber protein dengan enzim alkalase yang kemudian diekstraksi menggunakan reaktor membran enzimatis secara kontinu. Kondisi optimum untuk menghasilkan peptida adalah [E]/[S] sebesar 5%, pH 7,5, dan residence time 12 jam menggunakan membran 5 kDa MWCO dengan nilai kapasitas antioksidan metode DPPH sebesar 4,73x10-2 ± 1,37x10-3 µg AEAC/mL, metode FRAP sebesar 2,57x10-2 ± 1,12x10-3 µg AEAC/mL, dan persen inhibisi sebesar 78,56 ± 0,63. Permeat dengan fraksi protein <2 kDa dengan nilai IC50 terbaik sebesar 1,22x10-5 ± 4,67x10-6 mg/mL.
       
      Bioactive peptides derived from protein sources can be used as a source to produce functional food that has an effect on health. One of the vegetable proteins that has the potential as a source of bioactive peptides is velvet bean. This study aims to produce bioactive koro benguk peptides continuously using an enzymatic membrane reactor with optimum conditions. Bioactive peptides that have antioxidant activity can be produced by hydrolyzing protein sources with alkalase enzymes which are then extracted using an enzymatic membrane reactor continuously. The optimum conditions for producing peptides were [E]/[S] of 5%, pH 7.5, and residence time of 12 hours using a 5 kDa MWCO membrane with an antioxidant capacity value of the DPPH method of 4,73x10-2 ± 1,37x10-3 µg AEAC/mL, the FRAP method was 2,57x10-2 ± 1,12x10-3 µg AEAC/mL, and the percent inhibition was 78,56 ± 0,63. Permeate with a protein fraction <2 kDa with the best IC50 value of 1,22x10-5 ± 4,67x10-6 mg/mL.
       
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      http://repository.ipb.ac.id/handle/123456789/125799
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      • UT - Food Science and Technology [3623]

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