Abstract
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 70°C 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 F. islandicum AW-1. The enzyme exhibited activity toward casein and soluble keratin optimally at 100°C and pH 9, and had a half-life of 90 min at 100°C. 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 F. islandicum AW-1 is a novel, thermostable keratinolytic serine protease.
| Original language | English |
|---|---|
| Pages (from-to) | 538-547 |
| Number of pages | 10 |
| Journal | Archives of Microbiology |
| Volume | 178 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2002 Nov 26 |
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All Science Journal Classification (ASJC) codes
- Microbiology
- Biochemistry
- Molecular Biology
- Genetics
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Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe. / Nam, Gae Won; Lee, Dong Woo; Lee, Han Seoung; Lee, Nam Ju; Kim, Byoung Chan; Choe, Eun Ah; Hwang, Jae-Kwan; Suhartono, Maggy T.; Pyun, Yu Ryang.
In: Archives of Microbiology, Vol. 178, No. 6, 26.11.2002, p. 538-547.Research output: Contribution to journal › Article
TY - JOUR
T1 - Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe
AU - Nam, Gae Won
AU - Lee, Dong Woo
AU - Lee, Han Seoung
AU - Lee, Nam Ju
AU - Kim, Byoung Chan
AU - Choe, Eun Ah
AU - Hwang, Jae-Kwan
AU - Suhartono, Maggy T.
AU - Pyun, Yu Ryang
PY - 2002/11/26
Y1 - 2002/11/26
N2 - 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 70°C 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 F. islandicum AW-1. The enzyme exhibited activity toward casein and soluble keratin optimally at 100°C and pH 9, and had a half-life of 90 min at 100°C. 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 F. islandicum AW-1 is a novel, thermostable keratinolytic serine protease.
AB - 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 70°C 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 F. islandicum AW-1. The enzyme exhibited activity toward casein and soluble keratin optimally at 100°C and pH 9, and had a half-life of 90 min at 100°C. 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 F. islandicum AW-1 is a novel, thermostable keratinolytic serine protease.
UR - http://www.scopus.com/inward/record.url?scp=0036428747&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036428747&partnerID=8YFLogxK
U2 - 10.1007/s00203-002-0489-0
DO - 10.1007/s00203-002-0489-0
M3 - Article
C2 - 12420177
AN - SCOPUS:0036428747
VL - 178
SP - 538
EP - 547
JO - Archives of Microbiology
JF - Archives of Microbiology
SN - 0302-8933
IS - 6
ER -