Amity Institute of Microbial Biotechnology, Amity University, Sector-125, Noida, Uttar Pradesh India.
Indian J Microbiol. 2014 Dec;54(4):466-70. doi: 10.1007/s12088-014-0477-5. Epub 2014 Jun 18.
The keratinase degrade highly rigid, cross linked structural polypeptides with different efficiency depending on the type of source. Two newly isolated strains of Bacillus subtilis (RSE163 and RSE165; NCBI Accession no JQ887983 and JQ887982) were found to be efficient keratinase producers with unusual catalytic activity result in different morphological changes in degradation pattern of feather, confirmed by their scanned electron micrographs. Maximum keratinolytic activity of both the strains B. subtilis RSE163 and RSE165 were found to be 366 ± 15.79 and 194 ± 7.26 U after 72 h of incubation. While the disulphide reductase activity of RSE163 and RSE165 estimated 0.24 ± 0.05 and 0.15 ± 0.03 U/ml of enzyme after 24 h of incubation. A total of 16 free amino acids of variable concentration were also analyzed in the cell free supernatant of hydrolyzed feather from two strains. Present study demonstrates the action of two different keratinases in feather degradation.
两种新分离的枯草芽孢杆菌（RSE163 和 RSE165；NCBI 登录号 JQ887983 和 JQ887982）被发现是高效角蛋白酶产生菌，具有不同的催化活性，导致羽毛降解模式的形态发生不同的变化，这一点通过扫描电子显微镜得到了证实。在 72 小时的孵育后，两种枯草芽孢杆菌 RSE163 和 RSE165 的最大角蛋白酶活性分别为 366±15.79 和 194±7.26 U。而 RSE163 和 RSE165 的二硫键还原酶活性在孵育 24 小时后分别估计为 0.24±0.05 和 0.15±0.03 U/ml。在两种菌株水解羽毛的无细胞上清液中还分析了 16 种不同浓度的游离氨基酸。本研究表明了两种不同角蛋白酶在羽毛降解中的作用。
