Ebenezer Asiamah , Dominic Aboagye , Ahmed A. Zaky , Charles Asakiya , Ethel Juliet Serwa Blessie
{"title":"Enzymatic modification of Fish Gelatin and Beet Pectin using Horseradish peroxidase","authors":"Ebenezer Asiamah , Dominic Aboagye , Ahmed A. Zaky , Charles Asakiya , Ethel Juliet Serwa Blessie","doi":"10.1016/j.fhfh.2022.100080","DOIUrl":null,"url":null,"abstract":"<div><p>The Fish Gelatin (FG), a good alternative for unhealthy and limited socio-cultural mammalian gelatin appears to possess endogenous structural limitations. The goal of this work was to use enzymatic crosslinking to modify cold-water Fish Gelatin (FG) with Beet Pectin. Reaction conditions were optimized by a single factorial experiment and covalent crosslinking was measured by ultraviolet (UV)-Vis spectroscopy at 340 nm to indicate Horseradish Peroxidase (HRP) catalyzes Beet Pectin (BP). At 50 °C for 4 h, the highest weight ratio of heterologous adducts between FG-BP was 1:3, with HRP and Hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) of 2 µg/mL and 0.067%, (v/v), respectively. Intermolecular cross-linking was found between treated samples using ATR-FTIR and Sodium Dodecyl Sulphur and Polyacrylamide Gel Electrophoresis (SDS-PAGE). The heterologous product, control FG, and BP as well as a mixture of untreated FG-BP had a β-sheet of 41.14%, 39.65%, 39.9%, and 40.0%, respectively. The maximum reduction in elution was obtained in heterogeneous FG-BP complex. Furthermore, a schematic mechanism for Cold-water Fish Gelatin and Beet Pectin was proposed. Overall, peroxidase crosslinked BP was able to modify cold-water Fish Gelatin. The use of Horseradish peroxidase on Fish Gelatin could provide a practical way of building the FG-BP complex as a basis for understanding the FG functionalities comprehensively.</p></div>","PeriodicalId":12385,"journal":{"name":"Food Hydrocolloids for Health","volume":"2 ","pages":"Article 100080"},"PeriodicalIF":4.6000,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667025922000279/pdfft?md5=b18b5c4ee02315a448a664d4c300ce31&pid=1-s2.0-S2667025922000279-main.pdf","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids for Health","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2667025922000279","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 2
Abstract
The Fish Gelatin (FG), a good alternative for unhealthy and limited socio-cultural mammalian gelatin appears to possess endogenous structural limitations. The goal of this work was to use enzymatic crosslinking to modify cold-water Fish Gelatin (FG) with Beet Pectin. Reaction conditions were optimized by a single factorial experiment and covalent crosslinking was measured by ultraviolet (UV)-Vis spectroscopy at 340 nm to indicate Horseradish Peroxidase (HRP) catalyzes Beet Pectin (BP). At 50 °C for 4 h, the highest weight ratio of heterologous adducts between FG-BP was 1:3, with HRP and Hydrogen peroxide (H2O2) of 2 µg/mL and 0.067%, (v/v), respectively. Intermolecular cross-linking was found between treated samples using ATR-FTIR and Sodium Dodecyl Sulphur and Polyacrylamide Gel Electrophoresis (SDS-PAGE). The heterologous product, control FG, and BP as well as a mixture of untreated FG-BP had a β-sheet of 41.14%, 39.65%, 39.9%, and 40.0%, respectively. The maximum reduction in elution was obtained in heterogeneous FG-BP complex. Furthermore, a schematic mechanism for Cold-water Fish Gelatin and Beet Pectin was proposed. Overall, peroxidase crosslinked BP was able to modify cold-water Fish Gelatin. The use of Horseradish peroxidase on Fish Gelatin could provide a practical way of building the FG-BP complex as a basis for understanding the FG functionalities comprehensively.