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Wang, S., Lin, X., Huang, X., Zheng, L. and Zilda, D.S. (2012) Screening and characterization of the alkaline pro tease isolated from PLI-1, a strain of Brevibacillus sp. collected from Indonesia’s hot springs. Journal of Ocean University of China, 11, 213-218. doi:10.1007/s11802-012-1845-6

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• TITLE: Green recycling of chicken feather and sheep wool using the partially purified alkaline protease from Bacillus circulans L.

  AUTHORS: Eman Fathi Sharaf, Khadijah Al-Fadel

  KEYWORDS: Bacillus; Alkaline Protease; Ammonium Sulphate Precipitation; Characterization; Feather; Wool; Blood Stains

  JOURNAL NAME: Natural Science, Vol.5 No.6A, June 18, 2013

  ABSTRACT: The previously optimized crude alkaline protease from the haloalkaliphilic Bacillus circulans L. was partially purified using ammonium sulphate fractionation and dialysis. The best specific activity (27.7 U/mg protein) was obtained at 80% saturation. The optimum reaction temperature and reaction pH was 47℃ and 9, respectively. The enzyme activity was enhanced with Ca and K chlorides but suppressed with HgCl2 and EDTA. The partially purified protease showed strong proteolytic activity on sheep wool and chicken feather. Also, the enzyme was compatible with the common detergent Tide and could improve its cleaning power in removing blood stain. These findings support the application of the present alka-line protease in biotechnological industries.