Influence of ultrasound and enzymatic cross-linking on freeze-thaw stability and release properties of whey protein isolate hydrogel
ABSTRACT: This study investigated the effect of ultrasound and enzymatic cross-linking on the freeze-thaw (FT) stability and release properties of whey protein isolate hydrogels. We evaluated the FT stability by the changes in the microstructure, riboflavin retention, syneresis, water holding capaci...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2022-09-01
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| Series: | Journal of Dairy Science |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022030222003940 |
| _version_ | 1817995601044832256 |
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| author | Yanli Zhao Mi Yan Shiqi Xue Tiehua Zhang Xue Shen |
| author_facet | Yanli Zhao Mi Yan Shiqi Xue Tiehua Zhang Xue Shen |
| author_sort | Yanli Zhao |
| collection | DOAJ |
| description | ABSTRACT: This study investigated the effect of ultrasound and enzymatic cross-linking on the freeze-thaw (FT) stability and release properties of whey protein isolate hydrogels. We evaluated the FT stability by the changes in the microstructure, riboflavin retention, syneresis, water holding capacity (WHC), and texture of gels subjected to 3 FT cycles. High-intensity ultrasound (HUS) and transglutaminase (TGase)-mediated cross-linking improved the FT stability of whey protein isolate hydrogels loaded with riboflavin (WPISAR), as demonstrated by a more uniform and denser porous structure, significantly higher riboflavin retention, WHC, and textural properties, and lower syneresis after 3 FT cycles than those of untreated hydrogels. Furthermore, HUS- and TGase-mediated cross-linking decreased protein erosion and swelling ratio of WPISAR in simulated gastrointestinal fluids (SGIF) and reduced the riboflavin release rate in SGIF both with and without the addition of digestive enzymes. After 3 FT cycles, faster riboflavin release occurred due to a more porous structure induced by ice crystal formation compared with their unfrozen counterparts as detected by confocal laser scanning microscopy. High-intensity ultrasound- and TGase-mediated cross-linking alleviated the FT-induced faster riboflavin release rate in SGIF. High-intensity ultrasound- and TGase-treated gel samples showed that both diffusion and network erosion were responsible for riboflavin release regardless of FT. These results suggest that HUS- and TGase-mediated cross-linking improved the FT stability of WPISAR with a high riboflavin retention, and might be a good candidate as a controlled-release vehicle for riboflavin delivery to overcome undesired FT processing. |
| first_indexed | 2024-04-14T02:09:50Z |
| format | Article |
| id | doaj.art-f9fdca78080141e6b4efc0649b91e8ff |
| institution | Directory Open Access Journal |
| issn | 0022-0302 |
| language | English |
| last_indexed | 2024-04-14T02:09:50Z |
| publishDate | 2022-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Dairy Science |
| spelling | doaj.art-f9fdca78080141e6b4efc0649b91e8ff2022-12-22T02:18:33ZengElsevierJournal of Dairy Science0022-03022022-09-01105972537265Influence of ultrasound and enzymatic cross-linking on freeze-thaw stability and release properties of whey protein isolate hydrogelYanli Zhao0Mi Yan1Shiqi Xue2Tiehua Zhang3Xue Shen4Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun, 130062, ChinaDepartment of Food Science, College of Food Science and Engineering, Jilin University, Changchun, 130062, ChinaDepartment of Food Science, College of Food Science and Engineering, Jilin University, Changchun, 130062, ChinaDepartment of Food Science, College of Food Science and Engineering, Jilin University, Changchun, 130062, ChinaCorresponding author; Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun, 130062, ChinaABSTRACT: This study investigated the effect of ultrasound and enzymatic cross-linking on the freeze-thaw (FT) stability and release properties of whey protein isolate hydrogels. We evaluated the FT stability by the changes in the microstructure, riboflavin retention, syneresis, water holding capacity (WHC), and texture of gels subjected to 3 FT cycles. High-intensity ultrasound (HUS) and transglutaminase (TGase)-mediated cross-linking improved the FT stability of whey protein isolate hydrogels loaded with riboflavin (WPISAR), as demonstrated by a more uniform and denser porous structure, significantly higher riboflavin retention, WHC, and textural properties, and lower syneresis after 3 FT cycles than those of untreated hydrogels. Furthermore, HUS- and TGase-mediated cross-linking decreased protein erosion and swelling ratio of WPISAR in simulated gastrointestinal fluids (SGIF) and reduced the riboflavin release rate in SGIF both with and without the addition of digestive enzymes. After 3 FT cycles, faster riboflavin release occurred due to a more porous structure induced by ice crystal formation compared with their unfrozen counterparts as detected by confocal laser scanning microscopy. High-intensity ultrasound- and TGase-mediated cross-linking alleviated the FT-induced faster riboflavin release rate in SGIF. High-intensity ultrasound- and TGase-treated gel samples showed that both diffusion and network erosion were responsible for riboflavin release regardless of FT. These results suggest that HUS- and TGase-mediated cross-linking improved the FT stability of WPISAR with a high riboflavin retention, and might be a good candidate as a controlled-release vehicle for riboflavin delivery to overcome undesired FT processing.http://www.sciencedirect.com/science/article/pii/S0022030222003940whey proteinhigh-intensity ultrasoundtransglutaminasefreeze-thaw stabilityrelease property |
| spellingShingle | Yanli Zhao Mi Yan Shiqi Xue Tiehua Zhang Xue Shen Influence of ultrasound and enzymatic cross-linking on freeze-thaw stability and release properties of whey protein isolate hydrogel Journal of Dairy Science whey protein high-intensity ultrasound transglutaminase freeze-thaw stability release property |
| title | Influence of ultrasound and enzymatic cross-linking on freeze-thaw stability and release properties of whey protein isolate hydrogel |
| title_full | Influence of ultrasound and enzymatic cross-linking on freeze-thaw stability and release properties of whey protein isolate hydrogel |
| title_fullStr | Influence of ultrasound and enzymatic cross-linking on freeze-thaw stability and release properties of whey protein isolate hydrogel |
| title_full_unstemmed | Influence of ultrasound and enzymatic cross-linking on freeze-thaw stability and release properties of whey protein isolate hydrogel |
| title_short | Influence of ultrasound and enzymatic cross-linking on freeze-thaw stability and release properties of whey protein isolate hydrogel |
| title_sort | influence of ultrasound and enzymatic cross linking on freeze thaw stability and release properties of whey protein isolate hydrogel |
| topic | whey protein high-intensity ultrasound transglutaminase freeze-thaw stability release property |
| url | http://www.sciencedirect.com/science/article/pii/S0022030222003940 |
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