Novel recombinant cold-adapted alkaliphilic lipase (Glalip03) from Antarctic yeast, Glaciozyma antarctica PI12
The present study investigates a novel low-temperature adapted lipase, Glalip03, from Glaciozyma antarctica. The gene was codon-optimised, synthesised, and heterologously expressed in E. coli strain Origami™ B (DE3) as a fusion with thioredoxin (Trx) using a pET32b (+) expression vector. The recombi...
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| Format: | Article |
| Language: | English |
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Springer Science and Business Media Deutschland
2024
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| Online Access: | http://psasir.upm.edu.my/id/eprint/115733/ http://psasir.upm.edu.my/id/eprint/115733/1/115733.pdf |
| _version_ | 1848866850060894208 |
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| author | Matinja, Adamu Idris Ahmad Kamarudin, Nor Hafizah Leow, Adam Thean Chor Oslan, Siti Nurbaya |
| author_facet | Matinja, Adamu Idris Ahmad Kamarudin, Nor Hafizah Leow, Adam Thean Chor Oslan, Siti Nurbaya |
| author_sort | Matinja, Adamu Idris |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | The present study investigates a novel low-temperature adapted lipase, Glalip03, from Glaciozyma antarctica. The gene was codon-optimised, synthesised, and heterologously expressed in E. coli strain Origami™ B (DE3) as a fusion with thioredoxin (Trx) using a pET32b (+) expression vector. The recombinant Trx-Glalip03 was expressed successfully in a soluble form with 0.1 mM concentration of isopropyl β-D-thiogalactopyranoside (IPTG) at 25 °C and post-induction time of 4 h. A one-step Nickel Sepharose affinity chromatography technique was used to purify the recombinant Trx-Glalip03 with an average molecular size of around 53 kDa. The purified Trx-Glalip03 was catalytically active against the hydrolysis of triglycerides and olive oil with a preference for triolein, tripalmitin, and tributyrin. The Trx-Glalip03 showed high stability under different organic solvents with temperature and pH optimum at 30 °C and 9.0, respectively. Furthermore, the Trx-Glalip03 catalytic activity was similarly influenced by metal ions and ethylenediaminetetraacetic acid (EDTA). The kinetic behaviour of the lipase reaction was described with Hill equation kinetics resulting in a dissociation constant (Kd) value of 0.32 g/mL and positive hill coefficient (n). These biochemical features of the recombinant lipase Trx-Glalip03 suggest that it is an effective and innovative biocatalyst for biotechnological and industrial applications. |
| first_indexed | 2025-11-15T14:27:09Z |
| format | Article |
| id | upm-115733 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T14:27:09Z |
| publishDate | 2024 |
| publisher | Springer Science and Business Media Deutschland |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1157332025-03-13T03:04:52Z http://psasir.upm.edu.my/id/eprint/115733/ Novel recombinant cold-adapted alkaliphilic lipase (Glalip03) from Antarctic yeast, Glaciozyma antarctica PI12 Matinja, Adamu Idris Ahmad Kamarudin, Nor Hafizah Leow, Adam Thean Chor Oslan, Siti Nurbaya The present study investigates a novel low-temperature adapted lipase, Glalip03, from Glaciozyma antarctica. The gene was codon-optimised, synthesised, and heterologously expressed in E. coli strain Origami™ B (DE3) as a fusion with thioredoxin (Trx) using a pET32b (+) expression vector. The recombinant Trx-Glalip03 was expressed successfully in a soluble form with 0.1 mM concentration of isopropyl β-D-thiogalactopyranoside (IPTG) at 25 °C and post-induction time of 4 h. A one-step Nickel Sepharose affinity chromatography technique was used to purify the recombinant Trx-Glalip03 with an average molecular size of around 53 kDa. The purified Trx-Glalip03 was catalytically active against the hydrolysis of triglycerides and olive oil with a preference for triolein, tripalmitin, and tributyrin. The Trx-Glalip03 showed high stability under different organic solvents with temperature and pH optimum at 30 °C and 9.0, respectively. Furthermore, the Trx-Glalip03 catalytic activity was similarly influenced by metal ions and ethylenediaminetetraacetic acid (EDTA). The kinetic behaviour of the lipase reaction was described with Hill equation kinetics resulting in a dissociation constant (Kd) value of 0.32 g/mL and positive hill coefficient (n). These biochemical features of the recombinant lipase Trx-Glalip03 suggest that it is an effective and innovative biocatalyst for biotechnological and industrial applications. Springer Science and Business Media Deutschland 2024-11-05 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/115733/1/115733.pdf Matinja, Adamu Idris and Ahmad Kamarudin, Nor Hafizah and Leow, Adam Thean Chor and Oslan, Siti Nurbaya (2024) Novel recombinant cold-adapted alkaliphilic lipase (Glalip03) from Antarctic yeast, Glaciozyma antarctica PI12. Rendiconti Lincei, 35 (4). art. no. 100823. pp. 1013-1031. ISSN 2037-4631; eISSN: 2385-2623 https://link.springer.com/article/10.1007/s12210-024-01277-2?error=cookies_not_supported&code=a7734877-7a0a-46aa-a509-c1836d226dae 10.1007/s12210-024-01277-2 |
| spellingShingle | Matinja, Adamu Idris Ahmad Kamarudin, Nor Hafizah Leow, Adam Thean Chor Oslan, Siti Nurbaya Novel recombinant cold-adapted alkaliphilic lipase (Glalip03) from Antarctic yeast, Glaciozyma antarctica PI12 |
| title | Novel recombinant cold-adapted alkaliphilic lipase (Glalip03) from Antarctic yeast, Glaciozyma antarctica PI12 |
| title_full | Novel recombinant cold-adapted alkaliphilic lipase (Glalip03) from Antarctic yeast, Glaciozyma antarctica PI12 |
| title_fullStr | Novel recombinant cold-adapted alkaliphilic lipase (Glalip03) from Antarctic yeast, Glaciozyma antarctica PI12 |
| title_full_unstemmed | Novel recombinant cold-adapted alkaliphilic lipase (Glalip03) from Antarctic yeast, Glaciozyma antarctica PI12 |
| title_short | Novel recombinant cold-adapted alkaliphilic lipase (Glalip03) from Antarctic yeast, Glaciozyma antarctica PI12 |
| title_sort | novel recombinant cold-adapted alkaliphilic lipase (glalip03) from antarctic yeast, glaciozyma antarctica pi12 |
| url | http://psasir.upm.edu.my/id/eprint/115733/ http://psasir.upm.edu.my/id/eprint/115733/ http://psasir.upm.edu.my/id/eprint/115733/ http://psasir.upm.edu.my/id/eprint/115733/1/115733.pdf |