Structure modification of stirred fermented milk gel due to laccase-catalysed protein crosslinking in a post-processing step

摘要: Abstract Laccases are a promising candidate for crosslinking milk proteins in stirred fermented milks. It was applied post-processing step due to its acidic pH optimum reported literature rebodying of the gel and an improvement structure. A laccase preparation from Trametes versicolor had lower oxidation activity ultrafiltration permeate than model buffer systems, 4.5. skim gels but no significant change storage modulus or apparent viscosity yoghurt occurred. Confocal laser scanning micrographs showed more porous structure gel. Some fresh cheese samples improved rheological properties. competing peptidolytic assumed smaller peptides were detected acidified by fluorescence. Mass spectrometry returned mainly sequences. Although this does not exclude proteases, it indicates that radical mechanism laccases may lead protein degradation. Industrial Relevance Enzymatic modification can alter even create new structures. Rheological properties be via crosslinking, thus reducing costs addition powders stabilisers. An innovative approach combining biotechnology food science engineering is investigated. The study interesting both enzyme manufacturers dairy companies as aims at least partially fill knowledge gap between enzymology their real-world application products. However, enzymatic treatment additional also incurs which should taken into account.