Immobilized alcalase on ZIF-L as a biocatalyst for protein hydrolysis
Immobilization of alcalase on a ZIF-L (A@ZIF-L) support was explored for its potential application in producing hydrolysates of proteins extracted from microalgae. The immobilized enzyme was characterized using FTIR, XRD, SEM, and TGA, and the maximum adsorption capacity was found to be 672.1 ± 5.5...
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KeAi Communications Co., Ltd.
2025-06-01
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| Series: | Resources Chemicals and Materials |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2772443325000017 |
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| author | Hebah Al-Amodi Sajid Maqsood Sulaiman Al-Zuhair |
| author_facet | Hebah Al-Amodi Sajid Maqsood Sulaiman Al-Zuhair |
| author_sort | Hebah Al-Amodi |
| collection | DOAJ |
| description | Immobilization of alcalase on a ZIF-L (A@ZIF-L) support was explored for its potential application in producing hydrolysates of proteins extracted from microalgae. The immobilized enzyme was characterized using FTIR, XRD, SEM, and TGA, and the maximum adsorption capacity was found to be 672.1 ± 5.5 mg g⁻¹ at 40 °C. Adsorption equilibrium data indicated that alcalase physically adsorbed onto the ZIF-L, with the isotherm well described by the Freundlich model. The adsorption kinetics aligned best with the pseudo-first order model, suggesting that both film and intraparticle diffusion were significant. The hydrolytic activity of the immobilized A@ZIF-L was initially tested using BSA as a substrate. A diffusion-reaction model was developed and numerically solved to describe the reaction, with results confirming the presence of mass transfer limitations in the early stages of hydrolysis. The stability of the immobilized enzyme was demonstrated by retaining over 90 % of its initial activity after being stored at 4 °C for 70 days. Furthermore, the immobilized A@ZIF-L was used to hydrolyze protein extracts derived from Scenedesmus sp. microalgae. The bioactivity of the resulting protein hydrolysates was characterized, showing a total phenolic content of 29.1 ± 0.6 mg GAE g⁻¹ and a radical scavenging activity of 82.75 ± 2.20 %. These findings highlight the potential of Alcalase-based biocatalysts for applications in the food industry. |
| format | Article |
| id | doaj-art-e1d57bf40e7b46f28d500ee1a6fb21bb |
| institution | Kabale University |
| issn | 2772-4433 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | KeAi Communications Co., Ltd. |
| record_format | Article |
| series | Resources Chemicals and Materials |
| spelling | doaj-art-e1d57bf40e7b46f28d500ee1a6fb21bb2025-08-20T03:58:40ZengKeAi Communications Co., Ltd.Resources Chemicals and Materials2772-44332025-06-014210009110.1016/j.recm.2025.100091Immobilized alcalase on ZIF-L as a biocatalyst for protein hydrolysisHebah Al-Amodi0Sajid Maqsood1Sulaiman Al-Zuhair2Chemical and Petroleum Engineering Department, UAE University, 15551 Al Ain, UAEDepartment of Food Science, College of Agriculture and Veterinary Medicine, UAE University, 15551 Al Ain, UAEChemical and Petroleum Engineering Department, UAE University, 15551 Al Ain, UAE; Corresponding author.Immobilization of alcalase on a ZIF-L (A@ZIF-L) support was explored for its potential application in producing hydrolysates of proteins extracted from microalgae. The immobilized enzyme was characterized using FTIR, XRD, SEM, and TGA, and the maximum adsorption capacity was found to be 672.1 ± 5.5 mg g⁻¹ at 40 °C. Adsorption equilibrium data indicated that alcalase physically adsorbed onto the ZIF-L, with the isotherm well described by the Freundlich model. The adsorption kinetics aligned best with the pseudo-first order model, suggesting that both film and intraparticle diffusion were significant. The hydrolytic activity of the immobilized A@ZIF-L was initially tested using BSA as a substrate. A diffusion-reaction model was developed and numerically solved to describe the reaction, with results confirming the presence of mass transfer limitations in the early stages of hydrolysis. The stability of the immobilized enzyme was demonstrated by retaining over 90 % of its initial activity after being stored at 4 °C for 70 days. Furthermore, the immobilized A@ZIF-L was used to hydrolyze protein extracts derived from Scenedesmus sp. microalgae. The bioactivity of the resulting protein hydrolysates was characterized, showing a total phenolic content of 29.1 ± 0.6 mg GAE g⁻¹ and a radical scavenging activity of 82.75 ± 2.20 %. These findings highlight the potential of Alcalase-based biocatalysts for applications in the food industry.http://www.sciencedirect.com/science/article/pii/S2772443325000017AlcalaseProtein hydrolysisZeolitic imidazolate frameworkKinetics modellingBioactive peptides |
| spellingShingle | Hebah Al-Amodi Sajid Maqsood Sulaiman Al-Zuhair Immobilized alcalase on ZIF-L as a biocatalyst for protein hydrolysis Resources Chemicals and Materials Alcalase Protein hydrolysis Zeolitic imidazolate framework Kinetics modelling Bioactive peptides |
| title | Immobilized alcalase on ZIF-L as a biocatalyst for protein hydrolysis |
| title_full | Immobilized alcalase on ZIF-L as a biocatalyst for protein hydrolysis |
| title_fullStr | Immobilized alcalase on ZIF-L as a biocatalyst for protein hydrolysis |
| title_full_unstemmed | Immobilized alcalase on ZIF-L as a biocatalyst for protein hydrolysis |
| title_short | Immobilized alcalase on ZIF-L as a biocatalyst for protein hydrolysis |
| title_sort | immobilized alcalase on zif l as a biocatalyst for protein hydrolysis |
| topic | Alcalase Protein hydrolysis Zeolitic imidazolate framework Kinetics modelling Bioactive peptides |
| url | http://www.sciencedirect.com/science/article/pii/S2772443325000017 |
| work_keys_str_mv | AT hebahalamodi immobilizedalcalaseonziflasabiocatalystforproteinhydrolysis AT sajidmaqsood immobilizedalcalaseonziflasabiocatalystforproteinhydrolysis AT sulaimanalzuhair immobilizedalcalaseonziflasabiocatalystforproteinhydrolysis |