Characterization of enzymatically induced aggregation of casein micelles in natural concentration by in situ static light scattering and ultra low shear viscosimetry

D. Lehner, Peder Worning, Fritz G, Ogendal L, Bauer R, O. Glatter

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    The aggregation of casein micelles in undiluted skim milk after the addition of chymosin was studied bystatic light scattering and ultra low shear viscometry. The static light scattering measurements were madewith two different sample thicknesses, 72 and 16 mum. The scattering data were analyzed by indirect Fouriertransformation and by the polydispersity inversion technique which led to pair distance distributionfunctions and size distribution function, respectively. The minimum scattering angle was 1 degrees, whichallows for the determination of particle sizes up to a maximum diameter of 12 mum. The fractal dimensiondetermined from double logarithmic plots of intensity versus scattering vector resulted in values between 1.9and 2.0. The influence of multiple scattering was determined by comparison of the measurements with thedifferent sample thicknesses. The measurements show no significant influence of multiple scattering whenthe transmission is above 0.85. Due to the very complex and porous structure of the casein aggregates theRayleigh-Debye-Gans scattering theory has been used in the data analysis. Measurements with a newinstrument using ultra low shear showed good agreement with theory. Copyright 1999 Academic Press.
    Original languageEnglish
    JournalJournal of Colloid and Interface Science
    Volume213
    Issue number2
    Pages (from-to)445-456
    ISSN0021-9797
    Publication statusPublished - 1999

    Cite this