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 Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The study analysed mechanically deboned chicken meat subjected to washing and separation of fat and connective tissue in order to produce a preparation of myofibrillar proteins (MP). The preparation was modified using microbial transglutaminase (MTG). For this purpose, MP was supplemented with 3 g/kg MTG and modified at 6–7 °C for 5 h. Changes in the dynamics of water binding, which occurred in the course of heating and cooling within the temperature range of 20–70–20 °C, were analysed in the tested systems. Relaxation times   and   were determined using the low-field nuclear magnetic resonance (NMR). Enzymatic modification of MP and heating resulted in significant changes in the dynamics of bulk water binding in the tested protein systems. Due to the presence of transglutaminase in the preparation, the changes begin and end at lower temperatures. Analysis of relaxation time   showed that the addition of the enzyme to MP causes water binding in the sample up to 48 h after gel cooling. The addition of the enzyme to MP reduces the energy barrier determined, based on activation energy.

food and bioprocess technology

The Influence of Heating and Cooling Process on the Water Binding in Transglutaminase-Modified Chicken Protein Preparation, Assessed Using Low-Field NMR