Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite
Authorized Users Only
2024
Authors
Kosić, VišnjaBožić, Nataša
Dojnov, Biljana
Banković, Predrag
Jović-Jovičić, Nataša
Knežević-Jugović, Zorica
Milutinović-Nikolić, Aleksandra
Article (Published version)
Metadata
Show full item recordAbstract
Three glycoside hydrolases (α-amylase, xylanase and pullulanase) were immobilized on low-cost, environmentally friendly, easily modified clay rich in beidellite. Modifications included common procedures: Na-exchange, acid activation, pillaring, pillaring followed by acid activation, and organo-modifications with chitosan. Supports were characterized by chemical analysis, low temperature N2 physisorption, X-ray powder diffraction (XRPD) and Fourier-transform infrared (FT-IR) spectroscopy. The point of zero charge was also determined. Specific activity of different immobilizates of selected glycoside hydrolases was notably influenced by the type of chemical modification of supports. For each enzyme optimal support was chosen and storage stability was tested. α-Amylase immobilized on acid-activated support retained up to 95% of its initial specific activity of 105.6 ± 5.1 U g−1 after a testing period of 120 days. The most suitable support for xylanase was chitosan-modified beidellite with... having specific activity of 90.0 ± 1.4 U g−1 which retained >50% its value after 120 days. Specific activity of pullulanase immobilized on pillared sample that was subsequently activated by acid was 44.5 ± 0.7 U g−1. Initial activity was preserved up to 33% for the same testing period. Comparing these results to the storage stability of the free enzymes that completely lost their activity for the longest period of 40 days, it can be concluded that appropriately modified beidellite- based clays could be used as suitable supports for stabilization of glycoside hydrolases. Nevertheless, further characterization of immobilizates (pH, thermal and operational stability) is needed in order to raise the suitability for larger scale processes in food industry.
Keywords:
Beidellite / Immobilization / Modification / Pullulanase / Xylanase / α-amylaseSource:
Applied Clay Science, 03-2024, 250, 107289-Publisher:
- Elsevier Ltd.
Funding / projects:
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200026 (University of Belgrade, Institute of Chemistry, Technology and Metallurgy - IChTM) (RS-MESTD-inst-2020-200026)
- MultiPromis - Multifunctional leaf protein and assembled nanocarrier structures delivered by enzyme technology (RS-ScienceFundRS-Ideje-7751519)
Note:
- Supplementary information: https://technorep.tmf.bg.ac.rs/handle/123456789/7330
Related info:
- Referenced by
https://technorep.tmf.bg.ac.rs/handle/123456789/7330
Institution/Community
Tehnološko-metalurški fakultetTY - JOUR AU - Kosić, Višnja AU - Božić, Nataša AU - Dojnov, Biljana AU - Banković, Predrag AU - Jović-Jovičić, Nataša AU - Knežević-Jugović, Zorica AU - Milutinović-Nikolić, Aleksandra PY - 2024-03 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/7279 AB - Three glycoside hydrolases (α-amylase, xylanase and pullulanase) were immobilized on low-cost, environmentally friendly, easily modified clay rich in beidellite. Modifications included common procedures: Na-exchange, acid activation, pillaring, pillaring followed by acid activation, and organo-modifications with chitosan. Supports were characterized by chemical analysis, low temperature N2 physisorption, X-ray powder diffraction (XRPD) and Fourier-transform infrared (FT-IR) spectroscopy. The point of zero charge was also determined. Specific activity of different immobilizates of selected glycoside hydrolases was notably influenced by the type of chemical modification of supports. For each enzyme optimal support was chosen and storage stability was tested. α-Amylase immobilized on acid-activated support retained up to 95% of its initial specific activity of 105.6 ± 5.1 U g−1 after a testing period of 120 days. The most suitable support for xylanase was chitosan-modified beidellite with having specific activity of 90.0 ± 1.4 U g−1 which retained >50% its value after 120 days. Specific activity of pullulanase immobilized on pillared sample that was subsequently activated by acid was 44.5 ± 0.7 U g−1. Initial activity was preserved up to 33% for the same testing period. Comparing these results to the storage stability of the free enzymes that completely lost their activity for the longest period of 40 days, it can be concluded that appropriately modified beidellite- based clays could be used as suitable supports for stabilization of glycoside hydrolases. Nevertheless, further characterization of immobilizates (pH, thermal and operational stability) is needed in order to raise the suitability for larger scale processes in food industry. PB - Elsevier Ltd. T2 - Applied Clay Science T1 - Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite SP - 107289 VL - 250 DO - 10.1016/j.clay.2024.107289 ER -
@article{ author = "Kosić, Višnja and Božić, Nataša and Dojnov, Biljana and Banković, Predrag and Jović-Jovičić, Nataša and Knežević-Jugović, Zorica and Milutinović-Nikolić, Aleksandra", year = "2024-03", abstract = "Three glycoside hydrolases (α-amylase, xylanase and pullulanase) were immobilized on low-cost, environmentally friendly, easily modified clay rich in beidellite. Modifications included common procedures: Na-exchange, acid activation, pillaring, pillaring followed by acid activation, and organo-modifications with chitosan. Supports were characterized by chemical analysis, low temperature N2 physisorption, X-ray powder diffraction (XRPD) and Fourier-transform infrared (FT-IR) spectroscopy. The point of zero charge was also determined. Specific activity of different immobilizates of selected glycoside hydrolases was notably influenced by the type of chemical modification of supports. For each enzyme optimal support was chosen and storage stability was tested. α-Amylase immobilized on acid-activated support retained up to 95% of its initial specific activity of 105.6 ± 5.1 U g−1 after a testing period of 120 days. The most suitable support for xylanase was chitosan-modified beidellite with having specific activity of 90.0 ± 1.4 U g−1 which retained >50% its value after 120 days. Specific activity of pullulanase immobilized on pillared sample that was subsequently activated by acid was 44.5 ± 0.7 U g−1. Initial activity was preserved up to 33% for the same testing period. Comparing these results to the storage stability of the free enzymes that completely lost their activity for the longest period of 40 days, it can be concluded that appropriately modified beidellite- based clays could be used as suitable supports for stabilization of glycoside hydrolases. Nevertheless, further characterization of immobilizates (pH, thermal and operational stability) is needed in order to raise the suitability for larger scale processes in food industry.", publisher = "Elsevier Ltd.", journal = "Applied Clay Science", title = "Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite", pages = "107289", volume = "250", doi = "10.1016/j.clay.2024.107289" }
Kosić, V., Božić, N., Dojnov, B., Banković, P., Jović-Jovičić, N., Knežević-Jugović, Z.,& Milutinović-Nikolić, A.. (2024-03). Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. in Applied Clay Science Elsevier Ltd.., 250, 107289. https://doi.org/10.1016/j.clay.2024.107289
Kosić V, Božić N, Dojnov B, Banković P, Jović-Jovičić N, Knežević-Jugović Z, Milutinović-Nikolić A. Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite. in Applied Clay Science. 2024;250:107289. doi:10.1016/j.clay.2024.107289 .
Kosić, Višnja, Božić, Nataša, Dojnov, Biljana, Banković, Predrag, Jović-Jovičić, Nataša, Knežević-Jugović, Zorica, Milutinović-Nikolić, Aleksandra, "Significantly improved stabilization of glycoside hydrolases important in food industry by immobilization onto appropriately modified beidellite" in Applied Clay Science, 250 (2024-03):107289, https://doi.org/10.1016/j.clay.2024.107289 . .