Novel cross-linked enzyme aggregates of levanase from bacillus lehensis g1 for short-chain fructooligosaccharides synthesis: developmental, physicochemical, kinetic and thermodynamic properties
Short-chain fructooligosaccharides (scFOSs) can be produced from the levan hydrolysis using levanase. Levanase from Bacillus lehensis G1 (rlevblg1) is an enzyme that specifically converts levan to scFOSs. However, the use of free levanase presents a lack of stability and reusability, thus hindering...
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Elsevier B.V.
2020
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| _version_ | 1796865621413068800 |
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| author | Abd. Rahman, N. H. Jaafar, N. R. Abdul Murad, A. M. Abu Bakar, F. D. Shamsul Annuar, N. A. Md. Illias, R. |
| author_facet | Abd. Rahman, N. H. Jaafar, N. R. Abdul Murad, A. M. Abu Bakar, F. D. Shamsul Annuar, N. A. Md. Illias, R. |
| author_sort | Abd. Rahman, N. H. |
| collection | ePrints |
| description | Short-chain fructooligosaccharides (scFOSs) can be produced from the levan hydrolysis using levanase. Levanase from Bacillus lehensis G1 (rlevblg1) is an enzyme that specifically converts levan to scFOSs. However, the use of free levanase presents a lack of stability and reusability, thus hindering the synthesis of scFOSs for continuous reactions. Here, CLEAs for rlevblg1 were prepared and characterized. Cross-linked levanase aggregates using glutaraldehyde (CLLAs-ga) and bovine albumin serum (CLLAs-ga-bsa) showed the best activity recovery of 92.8% and 121.2%, respectively. The optimum temperature of CLLAs-ga and CLLAs-ga-bsa was increased to 35 °C and 40 °C, respectively, from its free rlevblg1 (30 °C). At high temperature (50 °C), the half-life of CLLAs-ga-bsa was higher than that of free rlevblg1 and CLLAs-ga. Both CLLAs exhibited higher stability at pH 9 and pH 10. Hyperactivation of CLLAs-ga-bsa was achieved with an effectiveness factor of more than 1 and with improved catalytic efficiency. After 3 h reaction, CLLAs-ga-bsa produced the highest total scFOSs yield of 35.4% and total sugar of 60.4% per gram levan. Finally, the reusability of CLLAs for 8 cycles with more than 50% activity retained makes them as a potential synthetic catalyst to be explored for scFOSs synthesis. |
| first_indexed | 2024-03-05T20:59:47Z |
| format | Article |
| id | utm.eprints-93437 |
| institution | Universiti Teknologi Malaysia - ePrints |
| last_indexed | 2024-03-05T20:59:47Z |
| publishDate | 2020 |
| publisher | Elsevier B.V. |
| record_format | dspace |
| spelling | utm.eprints-934372021-11-30T08:28:31Z http://eprints.utm.my/93437/ Novel cross-linked enzyme aggregates of levanase from bacillus lehensis g1 for short-chain fructooligosaccharides synthesis: developmental, physicochemical, kinetic and thermodynamic properties Abd. Rahman, N. H. Jaafar, N. R. Abdul Murad, A. M. Abu Bakar, F. D. Shamsul Annuar, N. A. Md. Illias, R. TP Chemical technology Short-chain fructooligosaccharides (scFOSs) can be produced from the levan hydrolysis using levanase. Levanase from Bacillus lehensis G1 (rlevblg1) is an enzyme that specifically converts levan to scFOSs. However, the use of free levanase presents a lack of stability and reusability, thus hindering the synthesis of scFOSs for continuous reactions. Here, CLEAs for rlevblg1 were prepared and characterized. Cross-linked levanase aggregates using glutaraldehyde (CLLAs-ga) and bovine albumin serum (CLLAs-ga-bsa) showed the best activity recovery of 92.8% and 121.2%, respectively. The optimum temperature of CLLAs-ga and CLLAs-ga-bsa was increased to 35 °C and 40 °C, respectively, from its free rlevblg1 (30 °C). At high temperature (50 °C), the half-life of CLLAs-ga-bsa was higher than that of free rlevblg1 and CLLAs-ga. Both CLLAs exhibited higher stability at pH 9 and pH 10. Hyperactivation of CLLAs-ga-bsa was achieved with an effectiveness factor of more than 1 and with improved catalytic efficiency. After 3 h reaction, CLLAs-ga-bsa produced the highest total scFOSs yield of 35.4% and total sugar of 60.4% per gram levan. Finally, the reusability of CLLAs for 8 cycles with more than 50% activity retained makes them as a potential synthetic catalyst to be explored for scFOSs synthesis. Elsevier B.V. 2020 Article PeerReviewed Abd. Rahman, N. H. and Jaafar, N. R. and Abdul Murad, A. M. and Abu Bakar, F. D. and Shamsul Annuar, N. A. and Md. Illias, R. (2020) Novel cross-linked enzyme aggregates of levanase from bacillus lehensis g1 for short-chain fructooligosaccharides synthesis: developmental, physicochemical, kinetic and thermodynamic properties. International Journal of Biological Macromolecules, 159 . pp. 577-589. ISSN 0141-8130 http://dx.doi.org/10.1016/j.ijbiomac.2020.04.262 DOI: 10.1016/j.ijbiomac.2020.04.262 |
| spellingShingle | TP Chemical technology Abd. Rahman, N. H. Jaafar, N. R. Abdul Murad, A. M. Abu Bakar, F. D. Shamsul Annuar, N. A. Md. Illias, R. Novel cross-linked enzyme aggregates of levanase from bacillus lehensis g1 for short-chain fructooligosaccharides synthesis: developmental, physicochemical, kinetic and thermodynamic properties |
| title | Novel cross-linked enzyme aggregates of levanase from bacillus lehensis g1 for short-chain fructooligosaccharides synthesis: developmental, physicochemical, kinetic and thermodynamic properties |
| title_full | Novel cross-linked enzyme aggregates of levanase from bacillus lehensis g1 for short-chain fructooligosaccharides synthesis: developmental, physicochemical, kinetic and thermodynamic properties |
| title_fullStr | Novel cross-linked enzyme aggregates of levanase from bacillus lehensis g1 for short-chain fructooligosaccharides synthesis: developmental, physicochemical, kinetic and thermodynamic properties |
| title_full_unstemmed | Novel cross-linked enzyme aggregates of levanase from bacillus lehensis g1 for short-chain fructooligosaccharides synthesis: developmental, physicochemical, kinetic and thermodynamic properties |
| title_short | Novel cross-linked enzyme aggregates of levanase from bacillus lehensis g1 for short-chain fructooligosaccharides synthesis: developmental, physicochemical, kinetic and thermodynamic properties |
| title_sort | novel cross linked enzyme aggregates of levanase from bacillus lehensis g1 for short chain fructooligosaccharides synthesis developmental physicochemical kinetic and thermodynamic properties |
| topic | TP Chemical technology |
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