Characterization of a kerationlytic metalloprotease from Bacillus sp. SCB-3 |
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| Authors: | H Lee D B Suh J H Hwang H J Suh |
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| Institution: | (1) Department of Food Science and Biotechnology, Kyonggi University, 442-760 Suwon, Konggi-do, Korea;(2) Doosan Corporation, 449-840 Yongin, Kyonggi-do, Korea;(3) Department of Kimchi and Food Science, Chongju National College of Science and Technology, 360-280 Chonju, Chungchongbuk-do, Korea;(4) Department of Food and Nutrition, College of Health Sciences, Korea University, 136-703 Sungbuk-ku, Seoul, Korea |
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| Abstract: | A keratinolytic protease-producing microorganism was isolated from soybean paste waste and was identified as a strain of Bacillus sp. The keratinase was purified by polyethylene glycol precipitation and two successive column chromatographies with DEAE-Toyopearl
650C and Sephacryl S-200 HR. The purified enzyme had overall 11 purification folds with an 18% yield. The results of sodium
dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration on Sephacryl G-200 indicated that the purified enzyme
was monomeric and had a molecular weight of 134 kDa. The optimum temperature and pH were 40°C and 7.0, respectively. This
enzyme was completely inhibited by EDTA and EGTA, and it was restored by the addition of Ca+2 and Mg+2. These results suggested that it is a metalloprotease. The stimulated enzyme activity by reducing agents indicated that the
reducing condition was important in the expression of the activity. |
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| Keywords: | Bacillus sp metalloprotease keratinolytic activity |
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