Please use this identifier to cite or link to this item: 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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