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Authors
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Abbate, R. A. ; Raak, N. ; Boye, S. ; Janke, A. ; Rohm, H. ; Jaros, D. ; Lederer, A.
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Title
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Asymmetric flow field flow fractionation for the investigation of caseins cross-linked by microbial transglutaminase
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Date
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28.03.2019
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Number
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56506
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Abstract
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The cross-linking of caseins with microbial transglutaminase (mTGase) was investigated using asymmetric flow field flow fractionation in combination with static and dynamic light scattering detections (AF4-MALS-DLS). This approach allows determining molar mass, molecular size, scaling properties, and apparent densities of casein aggregates prior to and after enzymatic treatment. The results show that, as a consequence of non-covalent interactions, casein molecules associate to form elongated aggregates with a molar mass () ranging from approx. 4·×·105 to 1.2·×·106·g·mol-1, and a mean radius of gyration () of approx. 16·nm. Upon enzymatic treatment with mTGase, casein aggregates become more compact as increases but decreases with ongoing cross-linking reaction. In contrast, the hydrodynamic radius distribution determined by online DLS is rather unaffected by enzymatic cross-linking, indicating that mTGase cross-links casein molecules mainly within distinct aggregates. Furthermore, extensive enzymatic treatments with mTGase change the molecular shapes of casein aggregates towards more compact and denser spherical structures.
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Publisher
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Food Hydrocolloids
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Wikidata
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Q108626294
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Citation
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Food Hydrocolloids 92 (2019) 117-124
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DOI
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https://doi.org/10.1016/J.FOODHYD.2019.01.043
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Tags
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casein cross-linking microbial transglutaminase asymmetric flow field flow fractionation light scattering scaling properties
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