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Recovery ofBacillus licheniformisAlkaline Protease from Supernatant of Fermented Wastewater Sludge Using Ultrafiltration and Its Characterization

机译:超滤法从发酵废水污泥上清液中分离地衣芽孢杆菌碱性蛋白酶及其表征

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Investigation on recovery of alkaline protease fromB. licheniformisATCC 21424 fermented wastewater sludge was carried out by centrifugation and ultrafiltration. Optimization of ultrafiltration parameters (transmembrane pressure (TMP) and feed flux) was carried out with 10 kDa membrane. TMP of 90 kPa and feed flux of 714 L/h/m2gave highest recovery (83%) of the enzyme from the centrifuged supernatant. The recovered enzyme had given maximum activity at temperature of 60°C and at pH 10. It was stable between pH 8 to 10 and retained 97% activity at 60°C after 180 min of incubation. Enzyme activity was significantly augmented by metal ions like Ca2+and Mn2+. Protease inhibitors like phenylmethyl sulphonyl fluoride (PMSF) and diisopropyl fluorophosphates (DFPs) completely inhibited the enzyme activity. The partially purified protease showed excellent stability and compatibility with various commercial detergents. The detergent (Sunlight) removed the blood stains effectively along with the enzyme as additive.
机译:从B中回收碱性蛋白酶的研究。地衣ATCC 21424发酵废水污泥通过离心和超滤进行。超滤参数(跨膜压(TMP)和进料通量)的优化是用10 kDa膜进行的。 TMP为90 kPa,进料流量为714 L / h / m2,可从离心的上清液中最高回收率(83%)。回收的酶在60°C的温度和10的pH值下具有最大的活性。孵育180分钟后,在8到10的pH值之间稳定,在60°C的条件下保留97%的活性。诸如Ca2 +和Mn2 +等金属离子显着增强了酶的活性。蛋白酶抑制剂,例如苯甲基磺酰氟(PMSF)和氟磷酸二异丙酯(DFP),完全抑制了酶的活性。部分纯化的蛋白酶显示出优异的稳定性和与各种市售洗涤剂的相容性。洗涤剂(阳光)与酶作为添加剂一起有效去除了血迹。

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