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https://hdl.handle.net/20.500.13087/846
Title: | ISOLATION, SCREENING, PARTIAL PURIFICATION AND CHARACTERIZATION OF PROTEASE FROM HALOPHILIC BACTERIA ISOLATED FROM INDONESIAN FERMENTED FOOD | Authors: | Fitriani, Sarah Güven, Kıymet |
Keywords: | Tarımsal Ekonomi ve Politika Ziraat Mühendisliği Bahçe Bitkileri Bitki Bilimleri Ziraat, Toprak Bilimi Biyoloji Çeşitliliğinin Korunması Biyoloji Kimya, Analitik Kimya, Uygulamalı Kimya, İnorganik ve Nükleer Kimya, Tıbbi Kimya, Organik Fizikokimya Ekoloji Entomoloji Çevre Bilimleri Balıkçılık Deniz ve Tatlı Su Biyolojisi Mikroskopi Mineraloji Mantar Bilimi Oşinografi Kuş Bilimi Paleontoloji Parazitoloji Fizik, Atomik ve Moleküler Kimya Fizik, Akışkanlar ve Plazma Spektroskopi İstatistik ve Olasılık Termodinamik Taşınım Viroloji Su Kaynakları Zooloji Hücre ve Doku Mühendisliği Çevre Mühendisliği Gıda Bilimi ve Teknolojisi Jeokimya ve Jeofizik Jeoloji Yeşil, Sürdürülebilir Bilim ve Teknoloji Denizcilik Maden İşletme ve Cevher Hazırlama Veterinerlik |
Issue Date: | 2018 | Abstract: | The protease producing bacteria were screened from Indonesian traditional fermented food, tauco and terasi, and 4 halophilic protease producers were isolated. Among these isolates, halophilic bacterial isolate TANN 4 was recorded as the best protease producer. Extracellular protease from isolate TANN 4 was partially purified using ammonium sulfate precipitation. The protease was partially purified with final yield of 72.87 % and 25.41 fold purity. This moderate thermoactive and alkaliphilic protease showed a pH optimum of 8.0 and temperature optimum was 50 °C. The enzyme was also active at salt concentrations ranging from 1 to 15 % (w/v), with optimum activity at 1 % NaCl (w/v). Ethylenediaminetetraacetic acid (EDTA) completely inhibited the enzyme activity suggesting that it was a metalloprotease. Among metal ions, the Ca2+, K+ and Mg2+ ions enhanced the activity of enzyme. The KM and Vmax values exhibited by partially purified protease were 0.0649 mM and 216.45 U mg?1 using casein as substrate. The molecular weight was estimated to be 19.8 kDa on SDS PAGE. The enzyme was also fairly stable in Triton X-100, SDS, 1 % commercial detergents (OMO and Ariel) and 25 % methanol and it was capable of hydrolyzing casein, hemoglobin and bovine serum albumin (BSA). These characteristics make this halophilic bacterial extracellular metalloprotease seem to be potentially useful for biotechnological and industrial applications. Automated ribotyping analysis revealed that 3 isolates (TANN 4, TR 2 and TR 4) resembled Halobacillus trueperi that exhibited 71, 68 and 69 % similarity respectively, and isolate (TR 1) resembled Virgibacillus pantothenticus with 64 % similarity. | URI: | https://doi.org/10.18036/aubtdc.322711 https://hdl.handle.net/20.500.13087/846 https://search.trdizin.gov.tr/yayin/detay/315964 |
ISSN: | 2146-0213 2146-0213 |
Appears in Collections: | Makine Mühendisliği Bölümü Koleksiyonu TR-Dizin İndeksli Yayınlar Koleksiyonu |
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