English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Previous reports have shown that egg white1} and its components, conalbumin2'3) and lysozyme,4) form gels by incubation with thiol reagents. This thiol-dependent gelation may be useful for improvement of the functionality of egg white as a food stuff. However, when a synthetic thiol reagent such as 2-mercaptoethanol is used, complete removal of the reagent is essential. Conversely, if a natural thiol is used, the retention of the reagent might be useful for textural or nutritional improvement of the protein. Therefore, it is important to determine whether thiol reagents are retained in or removed from the gel. In the present study, the gelation of conalbumin was studied using thiosalicylic acid as a model reagent, since it contains a carboxyl group, which is negatively charged at neutral or slightly alkaline pH, that is a condition required for the thiol-dependent gelation of conalbumin.3) Such a negative

Thiol-dependent gelation of conalbumin: Use of thiosalicylic acid and its removal from the gel.