View Item 
      •   IPB Repository
      • Dissertations and Theses
      • Undergraduate Theses
      • UT - Faculty of Animal Science
      • UT - Technology of Cattle Products
      • View Item
      •   IPB Repository
      • Dissertations and Theses
      • Undergraduate Theses
      • UT - Faculty of Animal Science
      • UT - Technology of Cattle Products
      • View Item
      JavaScript is disabled for your browser. Some features of this site may not work without it.

      Aktivitas Lipolitik Bakteri Asam Laktat Dari Daging Sapi Peranakan Ongole

      Thumbnail
      View/Open
      Cover (384.6Kb)
      Full text (6.689Mb)
      Lampiran (512.3Kb)
      Date
      2022
      Author
      Yanti, Hermarina Astifa
      Budiman, Cahyo
      Arief, Irma Isnafia
      Metadata
      Show full item record
      Abstract
      Selain kemampuannya sebagai strarter fermentasi, bakteri asam laktat (BAL) juga dikenal sebagai produsen enzim yang aplikatif di industri. Salah satu enzim yang dihasilkan oleh BAL adalah lipase, yaitu kelompok enzim yang menghidrolisis lemak (lipid), yang memiliki aplikasi yang luas di berbagai industri. Sebelumnya, 20 strain BAL telah diisolasi dari daging sapi segar lokal Peranakan Ongole (BAL-Ongole). Meskipun demikian, aktivitas lipase dari BAL tersebut belum diketahui. Tujuan penelitian ini adalah untuk mengetahui aktivitas lipolitik isolat BAL-Ongole. Dalam penelitian ini, 3 isolat BAL-Ongole dipilih sebagai representasi, yaitu Lactobacillus plantarum IIA-1A5, Enterococcus faecium 2D2, dan Pediococcus pentosaceus 2A2. Sebelum digunakan morfologi ketiga isolat tersebut dikonformasi dengan menggunakan pewarnaan Gram. Pengujian aktivitas lipase kemudian dilakukan dengan menggunakan metode sumur dengan menumbuhkan isolat tersebut pada MHA (Mueller Hinton Agar) yang ditambah Tributyrin 1% sebagai substrat lipase, kemudian diinkubasi dengan kondisi kedap udara (anaerob) pada suhu 37 ̊C selama 24 jam. Aktivitas lipase ditunjukkan dengan terbentuknya zona bening disekitar lubang sumur. Hasil menunjukkan bahwa E. faecium 2D2 memiliki aktivitas lebih tinggi dibandingkan kedua BAL lainnya. Aktivitas lipolitik tertinggi terlihat pada isolat E. faecium 2D2 sebesar 9,60 mm dengan kondisi optimum pada suhu 50 ̊C dan pH 9. Aktivitas spesifik enzim diketahui sebesar 0,016U/μL. Meskipun aktivitas lipolitik bakteri ini masih lebih rendah dari kontrol, akan tetapi proses pemurnian enzim ini diprediksi bisa meningkatkan aktivitasnya sebanding dengan kontrol.
       
      Apart from their widely-known ability as fermentation starters, lactic acid bacteria (LAB) is known to be the good producers for various enzyme, including lipase enzyme. This enzyme is able to catalyse the hydrolysis of lipid which are widely applicable in various industries. Earlier, 20 LAB isolates were optained from the fresh beef of Peranakan Ongole (LAB-Ongole), while these isolates are promising to be the good producers for lipase, their lipolytic activity have never been tested. This study aims to investigate the lipolytic activity of LAB-Ongole. For this purposes, 3 isolates of Ongole were used as representive, including Lactobacillus plantarum IIA-1A5, Enterococcus faecium 2D2, dan Pediococcus pentosaceus 2A2. The morphological-based purity of these isolates were confirmed using Gram staining prior to the lipolytic test. The tes was done using well-diffusion agar, whereby the isolate suspension was placed onto the well of MHA (Mueller Hilton Agar) with 1% Tributyrin as the lipase substrate. The agar wa then incubated at 37 ̊C for 24 h. The result showed that E. faecium 2D2 exhibited the highest lipolytic activity than the two other isolates. The optimum lipolytic activity of 2D2 isolate was 9,60 mm at 50 ̊C and pH 9. The specific activity of lipase from 2D2 isolate was found tobe 0,016 U/μL. While this activity was remarkably lower than the control (commercial lipase), the lipase of 2D2 enable the enzyme to exhibit the activity as high as the control. Although the lipolytic activity of these bacteria was still lower than the control, but the purification process of this enzyme was predicted to increase its activity comparable to the control.
       
      URI
      http://repository.ipb.ac.id/handle/123456789/111002
      Collections
      • UT - Technology of Cattle Products [266]

      Copyright © 2020 Library of IPB University
      All rights reserved
      Contact Us | Send Feedback
      Indonesia DSpace Group 
      IPB University Scientific Repository
      UIN Syarif Hidayatullah Institutional Repository
      Universitas Jember Digital Repository
        

       

      Browse

      All of IPB RepositoryCollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

      My Account

      Login

      Application

      google store

      Copyright © 2020 Library of IPB University
      All rights reserved
      Contact Us | Send Feedback
      Indonesia DSpace Group 
      IPB University Scientific Repository
      UIN Syarif Hidayatullah Institutional Repository
      Universitas Jember Digital Repository