Entrapment of Glucose Oxidase and Catalase in Silica–Calcium–Alginate Hydrogel Reduces the Release of Gluconic Acid in Must
Glucose oxidase (GOX) and catalase (CAT) were co-immobilized in silica–calcium–alginate hydrogels to degrade must glucose. The effect of the enzyme dose (1.2–2.4 U/mL), the initial must pH (3.6–4.0), and the incubation temperature (10–20 °C) on the glucose consumption, gluconic acid concentration, p...
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MDPI AG
2023-08-01
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Online Access: | https://www.mdpi.com/2310-2861/9/8/622 |
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author | David del-Bosque Josefina Vila-Crespo Violeta Ruipérez Encarnación Fernández-Fernández José Manuel Rodríguez-Nogales |
author_facet | David del-Bosque Josefina Vila-Crespo Violeta Ruipérez Encarnación Fernández-Fernández José Manuel Rodríguez-Nogales |
author_sort | David del-Bosque |
collection | DOAJ |
description | Glucose oxidase (GOX) and catalase (CAT) were co-immobilized in silica–calcium–alginate hydrogels to degrade must glucose. The effect of the enzyme dose (1.2–2.4 U/mL), the initial must pH (3.6–4.0), and the incubation temperature (10–20 °C) on the glucose consumption, gluconic acid concentration, pH, and color intensity of Verdejo must was studied by using a Box–Behnken experimental design and comparing free and co-immobilized enzymes. A reduction of up to 37.3 g/L of glucose was observed in co-immobilized enzyme-treated must, corresponding to a decrease in its potential alcohol strength of 2.0% vol. (<i>v</i>/<i>v</i>), while achieving a slight decrease in its pH (between 0.28 and 0.60). This slight acidification was due to a significant reduction in the estimated gluconic acid found in the must (up to 73.7%), likely due to its accumulation inside the capsules. Regarding the operational stability of immobilized enzymes, a gradual reduction in glucose consumption was observed over eight consecutive cycles. Finally, co-immobilized enzymes showed enhanced efficiency over a reaction period of 48 h, with an 87.1% higher ratio of glucose consumed per enzyme dose in the second 24 h period compared with free enzymes. These findings provide valuable insights into the performance of GOX–CAT co-immobilized to produce reduced-alcohol wines, mitigating excessive must acidification. |
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language | English |
last_indexed | 2024-03-10T23:54:56Z |
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series | Gels |
spelling | doaj.art-07ad0cf568c448878f7c6bea66506fbb2023-11-19T01:13:21ZengMDPI AGGels2310-28612023-08-019862210.3390/gels9080622Entrapment of Glucose Oxidase and Catalase in Silica–Calcium–Alginate Hydrogel Reduces the Release of Gluconic Acid in MustDavid del-Bosque0Josefina Vila-Crespo1Violeta Ruipérez2Encarnación Fernández-Fernández3José Manuel Rodríguez-Nogales4Área de Tecnología de los Alimentos, Escuela Técnica Superior de Ingenierías Agrarias, Universidad de Valladolid, 34004 Palencia, SpainÁrea de Microbiología, Escuela Técnica Superior de Ingenierías Agrarias, Universidad de Valladolid, 34004 Palencia, SpainÁrea de Microbiología, Escuela Técnica Superior de Ingenierías Agrarias, Universidad de Valladolid, 34004 Palencia, SpainÁrea de Tecnología de los Alimentos, Escuela Técnica Superior de Ingenierías Agrarias, Universidad de Valladolid, 34004 Palencia, SpainÁrea de Tecnología de los Alimentos, Escuela Técnica Superior de Ingenierías Agrarias, Universidad de Valladolid, 34004 Palencia, SpainGlucose oxidase (GOX) and catalase (CAT) were co-immobilized in silica–calcium–alginate hydrogels to degrade must glucose. The effect of the enzyme dose (1.2–2.4 U/mL), the initial must pH (3.6–4.0), and the incubation temperature (10–20 °C) on the glucose consumption, gluconic acid concentration, pH, and color intensity of Verdejo must was studied by using a Box–Behnken experimental design and comparing free and co-immobilized enzymes. A reduction of up to 37.3 g/L of glucose was observed in co-immobilized enzyme-treated must, corresponding to a decrease in its potential alcohol strength of 2.0% vol. (<i>v</i>/<i>v</i>), while achieving a slight decrease in its pH (between 0.28 and 0.60). This slight acidification was due to a significant reduction in the estimated gluconic acid found in the must (up to 73.7%), likely due to its accumulation inside the capsules. Regarding the operational stability of immobilized enzymes, a gradual reduction in glucose consumption was observed over eight consecutive cycles. Finally, co-immobilized enzymes showed enhanced efficiency over a reaction period of 48 h, with an 87.1% higher ratio of glucose consumed per enzyme dose in the second 24 h period compared with free enzymes. These findings provide valuable insights into the performance of GOX–CAT co-immobilized to produce reduced-alcohol wines, mitigating excessive must acidification.https://www.mdpi.com/2310-2861/9/8/622acidityhybrid capsuleorganic-inorganic gelsiliceous materialsol–gel network |
spellingShingle | David del-Bosque Josefina Vila-Crespo Violeta Ruipérez Encarnación Fernández-Fernández José Manuel Rodríguez-Nogales Entrapment of Glucose Oxidase and Catalase in Silica–Calcium–Alginate Hydrogel Reduces the Release of Gluconic Acid in Must Gels acidity hybrid capsule organic-inorganic gel siliceous material sol–gel network |
title | Entrapment of Glucose Oxidase and Catalase in Silica–Calcium–Alginate Hydrogel Reduces the Release of Gluconic Acid in Must |
title_full | Entrapment of Glucose Oxidase and Catalase in Silica–Calcium–Alginate Hydrogel Reduces the Release of Gluconic Acid in Must |
title_fullStr | Entrapment of Glucose Oxidase and Catalase in Silica–Calcium–Alginate Hydrogel Reduces the Release of Gluconic Acid in Must |
title_full_unstemmed | Entrapment of Glucose Oxidase and Catalase in Silica–Calcium–Alginate Hydrogel Reduces the Release of Gluconic Acid in Must |
title_short | Entrapment of Glucose Oxidase and Catalase in Silica–Calcium–Alginate Hydrogel Reduces the Release of Gluconic Acid in Must |
title_sort | entrapment of glucose oxidase and catalase in silica calcium alginate hydrogel reduces the release of gluconic acid in must |
topic | acidity hybrid capsule organic-inorganic gel siliceous material sol–gel network |
url | https://www.mdpi.com/2310-2861/9/8/622 |
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