Keratinolytic activity of Kocuria rosea

被引:36
作者
Bernal, C
Vidal, L
Valdivieso, E
Coello, N
机构
[1] Cent Univ Venezuela, Inst Expt Biol, Lab Biol Celular, Caracas 1041A, Venezuela
[2] Cent Univ Venezuela, Inst Expt Biol, Lab Proc Biotecnol, Caracas 1041A, Venezuela
[3] Univ Autonoma Barcelona, E-08193 Barcelona, Spain
关键词
carbon and nitrogen sources; keratinases; Kocuria rosea; poultry feather; proteases;
D O I
10.1023/A:1023685621215
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A strain of Kocuria rosea able to secrete keratin-hydrolysing proteinases (keratinases) in submerged batch cultures with finely milled feathers as carbon and nitrogen sources was studied. The highest production of keratinases was obtained when feathers were used as the only fermentation substrate ( 17 U/mg). Considerably lower activity was present in cultures containing glucose and others nutrient supplements. The optimum temperature and pH for keratinolytic activity was 40 degreesC and 10, respectively. Gelatin-sodiumdodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) electrophoresis analysis showed that Kocuria rosea grown on feathers secreted at least two alkaline extracellular proteases with apparent molecular weights of 90.2 and > 200 kDa, respectively. These proteolytic activities appear sequentially during microbial growth. Keratinolytic activity was strongly inhibited by phenylmethanesulphonyl fluoride (PMSF), chymostatin and crystalline soybean trypsin inhibitor, indicating the presence of serine proteases. Proteolytic enzymes derived from the biodegradation of feathers by this microorganism could be a useful biotechnological tool in the leather, food and cosmetic industries.
引用
收藏
页码:255 / 261
页数:7
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