Preliminary Study on Keratinase from Two Indonesian Isolates
Keratinases (E.C.3.4.99.11) constitute a group of enzymes capable of disrupting the highly stable keratin structure consisting of disulphide, hydrogen, and hydrophobic bonds in the form of α-helices and β-sheets B. licheniformis MB-2 and Bacillus sp. MTS are two feather-degrading bacteria isolated f...
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| Format: | Article |
| Language: | English |
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Universitas Jenderal Soedirman (UNSOED), Faculty of Animal Science
2010-01-01
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| Series: | Animal Production: Indonesian Journal of Animal Production |
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| Online Access: | http://animalproduction.net/index.php/JAP/article/view/281 |
| _version_ | 1827298159518285824 |
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| author | S Rahayu D Syah MT Suhartono |
| author_facet | S Rahayu D Syah MT Suhartono |
| author_sort | S Rahayu |
| collection | DOAJ |
| description | Keratinases (E.C.3.4.99.11) constitute a group of enzymes capable of disrupting the highly stable keratin structure consisting of disulphide, hydrogen, and hydrophobic bonds in the form of α-helices and β-sheets B. licheniformis MB-2 and Bacillus sp. MTS are two feather-degrading bacteria isolated from Tompaso crater at North Sulawesi and sulfuric land around Tangkuban Perahu in West Java. They were both capable of breaking down whole chicken feathers. In addition both isolates were capable of degrading other proteinous substrates rich in beta structure such as coccon, silk, human hair and fish scales. Result of fermentation experiment implied that addition of nitrogen sources (0.02% yeast extract and 0.02% tryptone) to the basal medium increased keratinase production. Our experiments showed that keratinase production of Bacillus sp. MTS was higher and faster than that from B. licheniformis MB-2. Maximum extracellular keratinase activity of the enzyme derived from B. licheniformis was obtained during stationary phase at 72 h, while Bacillus sp. MTS was reached at 48 h. Disulfide reductase activity also detected in the extracellular fluid of Bacillus sp. MTS. The maximum condition for extracellular keratinase activity was 55oC and the enzyme showed two maximum pHs : pH 8.0 and pH 10. The zymogram analysis indicated sixth protein bands of 17, 25, 32, 53, 96 and 122 kD which were able to hydrolyze gelatin substrate in-situ. (Animal Production 12(1): 60-68 (2010)Key Words : Bacillus, feather, keratinase, disulfide reductase |
| first_indexed | 2024-04-24T15:08:19Z |
| format | Article |
| id | doaj.art-3e1ef553e4aa46dd8e9d7ca08958699d |
| institution | Directory Open Access Journal |
| issn | 1411-2027 |
| language | English |
| last_indexed | 2024-04-24T15:08:19Z |
| publishDate | 2010-01-01 |
| publisher | Universitas Jenderal Soedirman (UNSOED), Faculty of Animal Science |
| record_format | Article |
| series | Animal Production: Indonesian Journal of Animal Production |
| spelling | doaj.art-3e1ef553e4aa46dd8e9d7ca08958699d2024-04-02T11:56:16ZengUniversitas Jenderal Soedirman (UNSOED), Faculty of Animal ScienceAnimal Production: Indonesian Journal of Animal Production1411-20272010-01-011216068Preliminary Study on Keratinase from Two Indonesian IsolatesS RahayuD SyahMT SuhartonoKeratinases (E.C.3.4.99.11) constitute a group of enzymes capable of disrupting the highly stable keratin structure consisting of disulphide, hydrogen, and hydrophobic bonds in the form of α-helices and β-sheets B. licheniformis MB-2 and Bacillus sp. MTS are two feather-degrading bacteria isolated from Tompaso crater at North Sulawesi and sulfuric land around Tangkuban Perahu in West Java. They were both capable of breaking down whole chicken feathers. In addition both isolates were capable of degrading other proteinous substrates rich in beta structure such as coccon, silk, human hair and fish scales. Result of fermentation experiment implied that addition of nitrogen sources (0.02% yeast extract and 0.02% tryptone) to the basal medium increased keratinase production. Our experiments showed that keratinase production of Bacillus sp. MTS was higher and faster than that from B. licheniformis MB-2. Maximum extracellular keratinase activity of the enzyme derived from B. licheniformis was obtained during stationary phase at 72 h, while Bacillus sp. MTS was reached at 48 h. Disulfide reductase activity also detected in the extracellular fluid of Bacillus sp. MTS. The maximum condition for extracellular keratinase activity was 55oC and the enzyme showed two maximum pHs : pH 8.0 and pH 10. The zymogram analysis indicated sixth protein bands of 17, 25, 32, 53, 96 and 122 kD which were able to hydrolyze gelatin substrate in-situ. (Animal Production 12(1): 60-68 (2010)Key Words : Bacillus, feather, keratinase, disulfide reductasehttp://animalproduction.net/index.php/JAP/article/view/281Bacillusfeatherkeratinasedisulfide reductase |
| spellingShingle | S Rahayu D Syah MT Suhartono Preliminary Study on Keratinase from Two Indonesian Isolates Animal Production: Indonesian Journal of Animal Production Bacillus feather keratinase disulfide reductase |
| title | Preliminary Study on Keratinase from Two Indonesian Isolates |
| title_full | Preliminary Study on Keratinase from Two Indonesian Isolates |
| title_fullStr | Preliminary Study on Keratinase from Two Indonesian Isolates |
| title_full_unstemmed | Preliminary Study on Keratinase from Two Indonesian Isolates |
| title_short | Preliminary Study on Keratinase from Two Indonesian Isolates |
| title_sort | preliminary study on keratinase from two indonesian isolates |
| topic | Bacillus feather keratinase disulfide reductase |
| url | http://animalproduction.net/index.php/JAP/article/view/281 |
| work_keys_str_mv | AT srahayu preliminarystudyonkeratinasefromtwoindonesianisolates AT dsyah preliminarystudyonkeratinasefromtwoindonesianisolates AT mtsuhartono preliminarystudyonkeratinasefromtwoindonesianisolates |