Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5T for raw starch hydrolysis
α-Amylase plays a crucial role in the industrial degradation of starch. The genus Jeotgalibacillus of the underexplored marine bacteria family Caryophanaceae has not been investigated in terms of α-amylase production. Herein, we report the comprehensive analysis of an α-amylase (AmyJM) from Jeotgali...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Springer Science and Business Media Deutschland GmbH
2024
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| Online Access: | http://psasir.upm.edu.my/id/eprint/115902/ http://psasir.upm.edu.my/id/eprint/115902/1/115902.pdf |
| _version_ | 1848866885218598912 |
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| author | Radzlin, Nurfatini Mohamad Ali, Mohd Shukuri Goh, Kian Mau Yaakop, Amira Suriaty Zakaria, Iffah Izzati Kahar, Ummirul Mukminin |
| author_facet | Radzlin, Nurfatini Mohamad Ali, Mohd Shukuri Goh, Kian Mau Yaakop, Amira Suriaty Zakaria, Iffah Izzati Kahar, Ummirul Mukminin |
| author_sort | Radzlin, Nurfatini |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | α-Amylase plays a crucial role in the industrial degradation of starch. The genus Jeotgalibacillus of the underexplored marine bacteria family Caryophanaceae has not been investigated in terms of α-amylase production. Herein, we report the comprehensive analysis of an α-amylase (AmyJM) from Jeotgalibacillus malaysiensis D5T (= DSM28777T = KCTC33550T). Protein phylogenetic analysis indicated that AmyJM belongs to glycoside hydrolase family 13 subfamily 5 (GH13_5) and exhibits low sequence identity with known α-amylases, with its closest counterpart being the GH13_5 α-amylase from Bacillus sp. KSM-K38 (51.05% identity). Purified AmyJM (molecular mass of 70 kDa) is stable at a pH range of 5.5–9.0 and optimally active at pH 7.5. The optimum temperature for AmyJM is 40 °C, where the enzyme is reasonably stable at this temperature. Similar to other α-amylases, the presence of CaCl2 enhanced both the activity and stability of AmyJM. AmyJM exhibited activity toward raw and gelatinized forms of starches and related α-glucans, generating a mixture of reducing sugars, such as glucose, maltose, maltotriose, maltotetraose, and maltopentaose. In raw starch hydrolysis, AmyJM exhibited its highest efficiency (51.10% degradation) in hydrolyzing raw wheat starch after 3-h incubation at 40 °C. Under the same conditions, AmyJM also hydrolyzed tapioca, sago, potato, rice, and corn raw starches, yielding 16.01–30.05%. These findings highlight the potential of AmyJM as a biocatalyst for the saccharification of raw starches, particularly those derived from wheat. |
| first_indexed | 2025-11-15T14:27:42Z |
| format | Article |
| id | upm-115902 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T14:27:42Z |
| publishDate | 2024 |
| publisher | Springer Science and Business Media Deutschland GmbH |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1159022025-03-14T00:18:08Z http://psasir.upm.edu.my/id/eprint/115902/ Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5T for raw starch hydrolysis Radzlin, Nurfatini Mohamad Ali, Mohd Shukuri Goh, Kian Mau Yaakop, Amira Suriaty Zakaria, Iffah Izzati Kahar, Ummirul Mukminin α-Amylase plays a crucial role in the industrial degradation of starch. The genus Jeotgalibacillus of the underexplored marine bacteria family Caryophanaceae has not been investigated in terms of α-amylase production. Herein, we report the comprehensive analysis of an α-amylase (AmyJM) from Jeotgalibacillus malaysiensis D5T (= DSM28777T = KCTC33550T). Protein phylogenetic analysis indicated that AmyJM belongs to glycoside hydrolase family 13 subfamily 5 (GH13_5) and exhibits low sequence identity with known α-amylases, with its closest counterpart being the GH13_5 α-amylase from Bacillus sp. KSM-K38 (51.05% identity). Purified AmyJM (molecular mass of 70 kDa) is stable at a pH range of 5.5–9.0 and optimally active at pH 7.5. The optimum temperature for AmyJM is 40 °C, where the enzyme is reasonably stable at this temperature. Similar to other α-amylases, the presence of CaCl2 enhanced both the activity and stability of AmyJM. AmyJM exhibited activity toward raw and gelatinized forms of starches and related α-glucans, generating a mixture of reducing sugars, such as glucose, maltose, maltotriose, maltotetraose, and maltopentaose. In raw starch hydrolysis, AmyJM exhibited its highest efficiency (51.10% degradation) in hydrolyzing raw wheat starch after 3-h incubation at 40 °C. Under the same conditions, AmyJM also hydrolyzed tapioca, sago, potato, rice, and corn raw starches, yielding 16.01–30.05%. These findings highlight the potential of AmyJM as a biocatalyst for the saccharification of raw starches, particularly those derived from wheat. Springer Science and Business Media Deutschland GmbH 2024-06-14 Article PeerReviewed text en cc_by_4 http://psasir.upm.edu.my/id/eprint/115902/1/115902.pdf Radzlin, Nurfatini and Mohamad Ali, Mohd Shukuri and Goh, Kian Mau and Yaakop, Amira Suriaty and Zakaria, Iffah Izzati and Kahar, Ummirul Mukminin (2024) Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5T for raw starch hydrolysis. AMB Express, 14 (1). art. no. 71. pp. 1-17. ISSN 2191-0855; eISSN: 2191-0855 https://amb-express.springeropen.com/articles/10.1186/s13568-024-01722-3 10.1186/s13568-024-01722-3 |
| spellingShingle | Radzlin, Nurfatini Mohamad Ali, Mohd Shukuri Goh, Kian Mau Yaakop, Amira Suriaty Zakaria, Iffah Izzati Kahar, Ummirul Mukminin Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5T for raw starch hydrolysis |
| title | Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5T for raw starch hydrolysis |
| title_full | Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5T for raw starch hydrolysis |
| title_fullStr | Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5T for raw starch hydrolysis |
| title_full_unstemmed | Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5T for raw starch hydrolysis |
| title_short | Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5T for raw starch hydrolysis |
| title_sort | exploring a novel gh13_5 α-amylase from jeotgalibacillus malaysiensis d5t for raw starch hydrolysis |
| url | http://psasir.upm.edu.my/id/eprint/115902/ http://psasir.upm.edu.my/id/eprint/115902/ http://psasir.upm.edu.my/id/eprint/115902/ http://psasir.upm.edu.my/id/eprint/115902/1/115902.pdf |