entrapment of porous cross-linked enzyme aggregates of maltogenic amylase from bacillus lehensis g1 into calcium alginate for maltooligosaccharides synthesis
Maltooligosaccharides (MOSs) are emerging oligosaccharides in food-based applications and can be synthesized through the enzymatic synthesis of maltogenic amylase from Bacillus lehensis G1 (Mag1). However, the lack of enzyme stability makes this approach unrealistic for industrial applications. The...
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2020
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my.utm.880522020-11-30T13:50:54Z http://eprints.utm.my/id/eprint/88052/ entrapment of porous cross-linked enzyme aggregates of maltogenic amylase from bacillus lehensis g1 into calcium alginate for maltooligosaccharides synthesis Nawawi, N. N. Hashim, Z. Rahman, R. A. Murad, A. M.A. Bakar, F. D. A. Illias, R. M. TP Chemical technology Maltooligosaccharides (MOSs) are emerging oligosaccharides in food-based applications and can be synthesized through the enzymatic synthesis of maltogenic amylase from Bacillus lehensis G1 (Mag1). However, the lack of enzyme stability makes this approach unrealistic for industrial applications. The formation of cross-linked enzyme aggregates (CLEAs) is a promising tool for improving enzyme stability, and the substrate accessibility problem of CLEA formation was overcome by the addition of porous agents to generate porous CLEAs (p-CLEAs). However, p-CLEAs exhibited high enzyme leaching and low solvent tolerance. To address these problems, p-CLEAs of Mag1 (Mag1-p-CLEAs) were entrapped in calcium alginate beads (CA). Mag1-p-CLEAs-CA prepared with 2.5% (w/v) sodium alginate and 0.6% (w/v) calcium chloride yielded 53.16% (17.0 U/mg) activity and showed a lower deactivation rate and longer half-life than those of entrapped free Mag1 (Mag1-CA) and entrapped non-porous Mag1-CLEAs (Mag1-CLEAs-CA). Moreover, Mag1-p-CLEAs-CA exhibited low enzyme leaching and high tolerance in various solvents compared to Mag1-p-CLEAs. A kinetic study revealed that Mag1-p-CLEAs-CA exhibited relatively high affinity towards beta-cyclodextrin (β-CD) (Km = 0.62 mM). MOSs (300 mg/g) were synthesized by Mag1-p-CLEAs-CA at 50 °C. Finally, the reusability of Mag1-p-CLEAs-CA makes them as a potential biocatalyst for the continuous synthesis of MOSs. Elsevier BV. 2020-05 Article PeerReviewed Nawawi, N. N. and Hashim, Z. and Rahman, R. A. and Murad, A. M.A. and Bakar, F. D. A. and Illias, R. M. (2020) entrapment of porous cross-linked enzyme aggregates of maltogenic amylase from bacillus lehensis g1 into calcium alginate for maltooligosaccharides synthesis. International Journal of Biological Macromolecules, 150 . pp. 80-89. ISSN 0141-8130 http://www.dx.doi.org/10.1016/j.ijbiomac.2020.02.032 DOI: 10.1016/j.ijbiomac.2020.02.032 |
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TP Chemical technology Nawawi, N. N. Hashim, Z. Rahman, R. A. Murad, A. M.A. Bakar, F. D. A. Illias, R. M. entrapment of porous cross-linked enzyme aggregates of maltogenic amylase from bacillus lehensis g1 into calcium alginate for maltooligosaccharides synthesis |
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Maltooligosaccharides (MOSs) are emerging oligosaccharides in food-based applications and can be synthesized through the enzymatic synthesis of maltogenic amylase from Bacillus lehensis G1 (Mag1). However, the lack of enzyme stability makes this approach unrealistic for industrial applications. The formation of cross-linked enzyme aggregates (CLEAs) is a promising tool for improving enzyme stability, and the substrate accessibility problem of CLEA formation was overcome by the addition of porous agents to generate porous CLEAs (p-CLEAs). However, p-CLEAs exhibited high enzyme leaching and low solvent tolerance. To address these problems, p-CLEAs of Mag1 (Mag1-p-CLEAs) were entrapped in calcium alginate beads (CA). Mag1-p-CLEAs-CA prepared with 2.5% (w/v) sodium alginate and 0.6% (w/v) calcium chloride yielded 53.16% (17.0 U/mg) activity and showed a lower deactivation rate and longer half-life than those of entrapped free Mag1 (Mag1-CA) and entrapped non-porous Mag1-CLEAs (Mag1-CLEAs-CA). Moreover, Mag1-p-CLEAs-CA exhibited low enzyme leaching and high tolerance in various solvents compared to Mag1-p-CLEAs. A kinetic study revealed that Mag1-p-CLEAs-CA exhibited relatively high affinity towards beta-cyclodextrin (β-CD) (Km = 0.62 mM). MOSs (300 mg/g) were synthesized by Mag1-p-CLEAs-CA at 50 °C. Finally, the reusability of Mag1-p-CLEAs-CA makes them as a potential biocatalyst for the continuous synthesis of MOSs. |
| format |
Article |
| author |
Nawawi, N. N. Hashim, Z. Rahman, R. A. Murad, A. M.A. Bakar, F. D. A. Illias, R. M. |
| author_facet |
Nawawi, N. N. Hashim, Z. Rahman, R. A. Murad, A. M.A. Bakar, F. D. A. Illias, R. M. |
| author_sort |
Nawawi, N. N. |
| title |
entrapment of porous cross-linked enzyme aggregates of maltogenic amylase from bacillus lehensis g1 into calcium alginate for maltooligosaccharides synthesis |
| title_short |
entrapment of porous cross-linked enzyme aggregates of maltogenic amylase from bacillus lehensis g1 into calcium alginate for maltooligosaccharides synthesis |
| title_full |
entrapment of porous cross-linked enzyme aggregates of maltogenic amylase from bacillus lehensis g1 into calcium alginate for maltooligosaccharides synthesis |
| title_fullStr |
entrapment of porous cross-linked enzyme aggregates of maltogenic amylase from bacillus lehensis g1 into calcium alginate for maltooligosaccharides synthesis |
| title_full_unstemmed |
entrapment of porous cross-linked enzyme aggregates of maltogenic amylase from bacillus lehensis g1 into calcium alginate for maltooligosaccharides synthesis |
| title_sort |
entrapment of porous cross-linked enzyme aggregates of maltogenic amylase from bacillus lehensis g1 into calcium alginate for maltooligosaccharides synthesis |
| publisher |
Elsevier BV. |
| publishDate |
2020 |
| url |
http://eprints.utm.my/id/eprint/88052/ http://www.dx.doi.org/10.1016/j.ijbiomac.2020.02.032 |
| _version_ |
1685579022306639872 |
| score |
13.211869 |