The influence of drying methods on extract content, tyrosinase activity inhibition, and mechanism in Ascophyllum nodosum: A combined microstructural and kinetic study
This study evaluates vacuum drying (VD), microwave drying (MD), hot air drying (HAD), and freeze drying (FD), on the color and microstructure changes of Ascophyllum nodosum (A. nodosum), which affect the extraction of polyphenols and flavonoids. During drying, VD and FD show slight color change and...
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| Published in | Food chemistry Vol. 458; p. 140230 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier Ltd
15.11.2024
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| Subjects | |
| Online Access | Get full text |
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| Abstract | This study evaluates vacuum drying (VD), microwave drying (MD), hot air drying (HAD), and freeze drying (FD), on the color and microstructure changes of Ascophyllum nodosum (A. nodosum), which affect the extraction of polyphenols and flavonoids. During drying, VD and FD show slight color change and looser structure, aiding in active compound preservation and extraction. Polyphenols extracted from A. nodosum (PEAn) using these methods show higher anti-tyrosinase activity, with VD treatment exhibiting the strongest inhibition. Kinetic studies demonstrate competitive inhibition between PEAn and tyrosinase. The binding constant (Ki) values indicate that PEAn treated with VD exhibits the most effective inhibition on tyrosinase, and the Zeta potential suggests the formation of the most stable complex. Circular dichroism (CD) spectroscopy shows significant enzyme rearrangement with VD-treated PEAn. Molecular docking confirms strong binding affinity. This study aims to enhance the utility of A. nodosum and develop novel uses for tyrosinase inhibitors in food.
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•Vacuum and freeze drying preserve Ascophyllum nodosum, enhancing polyphenol extraction.•Polyphenols extracted via vacuum drying exhibit potent anti-tyrosinase activity.•Kinetic studies reveal vacuum-dried polyphenols as most effective tyrosinase inhibitors.•Molecular docking confirms strong binding, suggesting potential food applications. |
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| AbstractList | This study evaluates vacuum drying (VD), microwave drying (MD), hot air drying (HAD), and freeze drying (FD), on the color and microstructure changes of Ascophyllum nodosum (A. nodosum), which affect the extraction of polyphenols and flavonoids. During drying, VD and FD show slight color change and looser structure, aiding in active compound preservation and extraction. Polyphenols extracted from A. nodosum (PEAn) using these methods show higher anti-tyrosinase activity, with VD treatment exhibiting the strongest inhibition. Kinetic studies demonstrate competitive inhibition between PEAn and tyrosinase. The binding constant (Ki) values indicate that PEAn treated with VD exhibits the most effective inhibition on tyrosinase, and the Zeta potential suggests the formation of the most stable complex. Circular dichroism (CD) spectroscopy shows significant enzyme rearrangement with VD-treated PEAn. Molecular docking confirms strong binding affinity. This study aims to enhance the utility of A. nodosum and develop novel uses for tyrosinase inhibitors in food.This study evaluates vacuum drying (VD), microwave drying (MD), hot air drying (HAD), and freeze drying (FD), on the color and microstructure changes of Ascophyllum nodosum (A. nodosum), which affect the extraction of polyphenols and flavonoids. During drying, VD and FD show slight color change and looser structure, aiding in active compound preservation and extraction. Polyphenols extracted from A. nodosum (PEAn) using these methods show higher anti-tyrosinase activity, with VD treatment exhibiting the strongest inhibition. Kinetic studies demonstrate competitive inhibition between PEAn and tyrosinase. The binding constant (Ki) values indicate that PEAn treated with VD exhibits the most effective inhibition on tyrosinase, and the Zeta potential suggests the formation of the most stable complex. Circular dichroism (CD) spectroscopy shows significant enzyme rearrangement with VD-treated PEAn. Molecular docking confirms strong binding affinity. This study aims to enhance the utility of A. nodosum and develop novel uses for tyrosinase inhibitors in food. This study evaluates vacuum drying (VD), microwave drying (MD), hot air drying (HAD), and freeze drying (FD), on the color and microstructure changes of Ascophyllum nodosum (A. nodosum), which affect the extraction of polyphenols and flavonoids. During drying, VD and FD show slight color change and looser structure, aiding in active compound preservation and extraction. Polyphenols extracted from A. nodosum (PEAn) using these methods show higher anti-tyrosinase activity, with VD treatment exhibiting the strongest inhibition. Kinetic studies demonstrate competitive inhibition between PEAn and tyrosinase. The binding constant (Ki) values indicate that PEAn treated with VD exhibits the most effective inhibition on tyrosinase, and the Zeta potential suggests the formation of the most stable complex. Circular dichroism (CD) spectroscopy shows significant enzyme rearrangement with VD-treated PEAn. Molecular docking confirms strong binding affinity. This study aims to enhance the utility of A. nodosum and develop novel uses for tyrosinase inhibitors in food. [Display omitted] •Vacuum and freeze drying preserve Ascophyllum nodosum, enhancing polyphenol extraction.•Polyphenols extracted via vacuum drying exhibit potent anti-tyrosinase activity.•Kinetic studies reveal vacuum-dried polyphenols as most effective tyrosinase inhibitors.•Molecular docking confirms strong binding, suggesting potential food applications. This study evaluates vacuum drying (VD), microwave drying (MD), hot air drying (HAD), and freeze drying (FD), on the color and microstructure changes of Ascophyllum nodosum (A. nodosum), which affect the extraction of polyphenols and flavonoids. During drying, VD and FD show slight color change and looser structure, aiding in active compound preservation and extraction. Polyphenols extracted from A. nodosum (PEAn) using these methods show higher anti-tyrosinase activity, with VD treatment exhibiting the strongest inhibition. Kinetic studies demonstrate competitive inhibition between PEAn and tyrosinase. The binding constant (K ) values indicate that PEAn treated with VD exhibits the most effective inhibition on tyrosinase, and the Zeta potential suggests the formation of the most stable complex. Circular dichroism (CD) spectroscopy shows significant enzyme rearrangement with VD-treated PEAn. Molecular docking confirms strong binding affinity. This study aims to enhance the utility of A. nodosum and develop novel uses for tyrosinase inhibitors in food. |
| ArticleNumber | 140230 |
| Author | Lu, Yujing Sun, Kailing Liu, Yu Guo, Sainan Wang, Yuze Qi, Hang Wang, Yuting |
| Author_xml | – sequence: 1 givenname: Yujing surname: Lu fullname: Lu, Yujing – sequence: 2 givenname: Yuting surname: Wang fullname: Wang, Yuting – sequence: 3 givenname: Yu surname: Liu fullname: Liu, Yu – sequence: 4 givenname: Yuze surname: Wang fullname: Wang, Yuze – sequence: 5 givenname: Sainan surname: Guo fullname: Guo, Sainan – sequence: 6 givenname: Kailing surname: Sun fullname: Sun, Kailing – sequence: 7 givenname: Hang surname: Qi fullname: Qi, Hang email: qihang@dlpu.edu.cn |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/38954954$$D View this record in MEDLINE/PubMed |
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| Keywords | Kinetic study Drying methods Molecular docking Ascophyllum nodosum Antityrosinase activity |
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| Title | The influence of drying methods on extract content, tyrosinase activity inhibition, and mechanism in Ascophyllum nodosum: A combined microstructural and kinetic study |
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