Effect of pigskin gelatin on baking, structural and thermal properties of frozen dough: Comprehensive studies on alteration of gluten network
Effect of pigskin gelatin and its hydrolysates on overall changes that frozen dough underwent during storage was investigated. The results showed that gelatin from pigskin could fortified the frozen dough bread quality, embodying in larger bread volume, softer and more uniform bread crumb. Impact of...
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Veröffentlicht in: | Food hydrocolloids 2020-05, Vol.102, p.105591, Article 105591 |
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Sprache: | eng |
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Zusammenfassung: | Effect of pigskin gelatin and its hydrolysates on overall changes that frozen dough underwent during storage was investigated. The results showed that gelatin from pigskin could fortified the frozen dough bread quality, embodying in larger bread volume, softer and more uniform bread crumb. Impact of pigskin gelatin on changes in the structure of gluten network in frozen dough was evaluated by different techniques. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) showed gelatin may inhibit the crosslinking of HMW macromolecules and entangle with SDS-soluble LMW proteins. The increased SDS-soluble proteins suggested a lower aggregation extent of glutenin macropolymer (GMP) caused by pigskin gelatin. However, the significant reduction in GMP depolymerization degree and thiol groups (-SH) content after 60-day frozen storage in presence of gelatin indicated the formation of a more resistant gluten structure against the distortion of ice crystals. There were no significant differences in the alteration of secondary structure and high-temperature stability between gelatin-depleted and gelatin-fortified groups. Nevertheless, the effect of pigskin gelatin on qualities of frozen dough was independent on its hydrolysis degree.
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•Gelatin from pigskin fortified the frozen dough bread quality.•Effect of pigskin gelatin on qualities of frozen dough was independent on its hydrolysis degree.•Pigskin gelatin resulted in a lower aggregation extent of glutenin macropolymer.•Gelatin inhibited the crosslinking of HMW macromolecules and entangle with SDS-soluble LMW proteins. |
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ISSN: | 0268-005X 1873-7137 |
DOI: | 10.1016/j.foodhyd.2019.105591 |