An impact of N-glycosylation on biochemical properties of a recombinant α-amylase from Bacillus licheniformis
Amylases are enzymes that are known to hydrolyze starch. High efficiency of amylolytic enzymes allows them to compete in the industry with the technology of chemical hydrolysis of starch. A Bacillus licheniformis strain with high amylolytic activity was isolated from soil and designated as T5. The g...
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| Format: | Article |
| Language: | English |
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Elsevier
2024-03-01
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| Series: | Heliyon |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405844024040957 |
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| author | Assel Kiribayeva Dmitriy Silayev Zhiger Akishev Kairat Baltin Saniya Aktayeva Yerlan Ramankulov Bekbolat Khassenov |
| author_facet | Assel Kiribayeva Dmitriy Silayev Zhiger Akishev Kairat Baltin Saniya Aktayeva Yerlan Ramankulov Bekbolat Khassenov |
| author_sort | Assel Kiribayeva |
| collection | DOAJ |
| description | Amylases are enzymes that are known to hydrolyze starch. High efficiency of amylolytic enzymes allows them to compete in the industry with the technology of chemical hydrolysis of starch. A Bacillus licheniformis strain with high amylolytic activity was isolated from soil and designated as T5. The gene encoding α-amylase from B. licheniformis T5 was successfully expressed in both Escherichia coli (rAmyT5-E) and Pichia pastoris (as rAmyT5-P). According to the study, the recombinant α-amylases rAmyT5-E and rAmyT5-P exhibited the highest activity at pH 6.0 and temperatures of 70 and 80 °C, respectively. Over 80% of the rAmyT5-E enzyme activity was preserved following incubation within the pH range of 5–9; the same was true for rAmyT5-P after incubation at pH 6–9. N-glycosylation reduced the thermal and pH stability of the enzyme. The specific activity and catalytic efficiency of the recombinant AmyT5 α-amylase were also diminished by N-glycosylation. |
| first_indexed | 2024-04-24T13:48:35Z |
| format | Article |
| id | doaj.art-bae8230606a8495c8d56c5aa60b3eddd |
| institution | Directory Open Access Journal |
| issn | 2405-8440 |
| language | English |
| last_indexed | 2024-04-24T13:48:35Z |
| publishDate | 2024-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Heliyon |
| spelling | doaj.art-bae8230606a8495c8d56c5aa60b3eddd2024-04-04T05:06:44ZengElsevierHeliyon2405-84402024-03-01106e28064An impact of N-glycosylation on biochemical properties of a recombinant α-amylase from Bacillus licheniformisAssel Kiribayeva0Dmitriy Silayev1Zhiger Akishev2Kairat Baltin3Saniya Aktayeva4Yerlan Ramankulov5Bekbolat Khassenov6National Center for Biotechnology, 13/5 Kurgalzhynskoye Road, Astana, 010000, KazakhstanNational Center for Biotechnology, 13/5 Kurgalzhynskoye Road, Astana, 010000, KazakhstanNational Center for Biotechnology, 13/5 Kurgalzhynskoye Road, Astana, 010000, KazakhstanNational Center for Biotechnology, 13/5 Kurgalzhynskoye Road, Astana, 010000, KazakhstanNational Center for Biotechnology, 13/5 Kurgalzhynskoye Road, Astana, 010000, KazakhstanNational Center for Biotechnology, 13/5 Kurgalzhynskoye Road, Astana, 010000, KazakhstanCorresponding author.; National Center for Biotechnology, 13/5 Kurgalzhynskoye Road, Astana, 010000, KazakhstanAmylases are enzymes that are known to hydrolyze starch. High efficiency of amylolytic enzymes allows them to compete in the industry with the technology of chemical hydrolysis of starch. A Bacillus licheniformis strain with high amylolytic activity was isolated from soil and designated as T5. The gene encoding α-amylase from B. licheniformis T5 was successfully expressed in both Escherichia coli (rAmyT5-E) and Pichia pastoris (as rAmyT5-P). According to the study, the recombinant α-amylases rAmyT5-E and rAmyT5-P exhibited the highest activity at pH 6.0 and temperatures of 70 and 80 °C, respectively. Over 80% of the rAmyT5-E enzyme activity was preserved following incubation within the pH range of 5–9; the same was true for rAmyT5-P after incubation at pH 6–9. N-glycosylation reduced the thermal and pH stability of the enzyme. The specific activity and catalytic efficiency of the recombinant AmyT5 α-amylase were also diminished by N-glycosylation.http://www.sciencedirect.com/science/article/pii/S2405844024040957α-AmylaseN-GlycosylationBacillus licheniformisPichia pastorisHydrolysis |
| spellingShingle | Assel Kiribayeva Dmitriy Silayev Zhiger Akishev Kairat Baltin Saniya Aktayeva Yerlan Ramankulov Bekbolat Khassenov An impact of N-glycosylation on biochemical properties of a recombinant α-amylase from Bacillus licheniformis Heliyon α-Amylase N-Glycosylation Bacillus licheniformis Pichia pastoris Hydrolysis |
| title | An impact of N-glycosylation on biochemical properties of a recombinant α-amylase from Bacillus licheniformis |
| title_full | An impact of N-glycosylation on biochemical properties of a recombinant α-amylase from Bacillus licheniformis |
| title_fullStr | An impact of N-glycosylation on biochemical properties of a recombinant α-amylase from Bacillus licheniformis |
| title_full_unstemmed | An impact of N-glycosylation on biochemical properties of a recombinant α-amylase from Bacillus licheniformis |
| title_short | An impact of N-glycosylation on biochemical properties of a recombinant α-amylase from Bacillus licheniformis |
| title_sort | impact of n glycosylation on biochemical properties of a recombinant α amylase from bacillus licheniformis |
| topic | α-Amylase N-Glycosylation Bacillus licheniformis Pichia pastoris Hydrolysis |
| url | http://www.sciencedirect.com/science/article/pii/S2405844024040957 |
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