Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe

被引:184
作者
Nam, GW
Lee, DW
Lee, HS
Lee, NJ
Kim, BC
Choe, EA
Hwang, JK
Suhartono, MT
Pyun, YR
机构
[1] Yonsei Univ, Dept Biotechnol, Seodaemun Gu, Seoul 120749, South Korea
[2] Yonsei Univ, Coll Engn, Bioprod Res Ctr, Seodaemun Gu, Seoul 120749, South Korea
[3] Bogor Agr Univ, Inter Univ Ctr Biotechnol, Bogor, Indonesia
关键词
native feathers; thermophilic anaerobe; Fervidobacterium islandicum AW-1; thermostable keratinolytic protease;
D O I
10.1007/s00203-002-0489-0
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A native-feather-degrading thermophilic anaerobe was isolated from a geothermal hot stream in Indonesia. Isolate AW-1, identified as a member of the species Fervidobacterium islandicum, was shown to degrade native feathers (0.8%, w/v) completely at 70degreesC and pH 7 with a maximum specific growth rate (0.14 h(-1)) in Thermotoga-Fervidobacterium (TF) medium. After 24 h of culture, feather degradation led to an increase in free amino acids such as histidine, cysteine and lysine. Moreover, nutritionally essential amino acids such as tryptophan and methionine, which are rare in feather keratin, were also produced as microbial metabolites. A homomultimeric membrane-bound keratinolytic protease (>200 kDa; 97 kDa subunits) was purified from a cell extract of E islandicum AW-1. The enzyme exhibited activity toward casein and soluble keratin optimally at 100degreesC and pH 9, and had a half-life of 90 min at 100degreesC. The enzyme showed higher specific activity for the keratinous substrates than other proteases and catalyzed the cleavage of peptide bonds more rapidly following the reduction of disulfide bridges in feather keratin by 10 mM dithiothreitol. Therefore, the enzyme from E islandicum AW-1 is a novel, thermostable keratinolytic serine protease.
引用
收藏
页码:538 / 547
页数:10
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