Authors: KunNan Chen JuChieh Huang ChingI Chung WenYen Kuo MingJu Chen
Publish Date: 2010/06/06
Volume: 27, Issue: 2, Pages: 349-358
Abstract
Two types of extracellular proteases with molecular mass of 500 and 448 kDa were found in H10 enzymes partially purified from Bacillus cereus H10 Further identification using liquid chromatographytandem mass spectrometry the enzyme with 500 kDa was identified as being similar to leucine dehydrogenase while the enzyme with 448 kDa might be a novel keratinolytic enzyme with little similarity to other proteins To maximize the keratinolytic and proteolytic abilities in the H10 enzymes a combination of response surface methodology and sequential quadratic programming technique was used to study the hydrolytic pH and temperature Results showed that the H10 enzymes could produce optimal proteolytic and keratinolytic activities at a hydrolysis temperature of 59°C at pH 757 Testing the protease activity on various protein substrates and temperatures indicated that the H10 enzymes showed high thermal stability and were very effective in porcine hair
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