2004
DOI: 10.1016/j.powtec.2003.10.009
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Fine milling and micronization of organic and inorganic materials under dynamic conditions

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Cited by 12 publications
(8 citation statements)
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“…These changes depend on the initial particle size, acceleration, angle and number of collisions as well as rotor's speed (Herceg et al, 2004a;Herceg, Lelas, Brn ci c, Tripalo, & Je zek, 2004b;Herceg, Lelas, & Skreblin, 2002;Lelas, 1998). The results obtained in this research have shown a significant decrease in particle size of all investigated materials (Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…These changes depend on the initial particle size, acceleration, angle and number of collisions as well as rotor's speed (Herceg et al, 2004a;Herceg, Lelas, Brn ci c, Tripalo, & Je zek, 2004b;Herceg, Lelas, & Skreblin, 2002;Lelas, 1998). The results obtained in this research have shown a significant decrease in particle size of all investigated materials (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…The wrinkled intramolecular structure of these proteins is a result of the disulfide bonds (S-S) between the remains of cisteine inside the molecules, mainly covered with hydrophobic remains (Tratnik, 1998). During TMA treatment of the materials, the protein globules (WPC) and casein micelles (SMP) were mechanically divided, producing a larger number of protein fragments and peptides, and the most significant changes occurred in the three-dimensional structures of globular proteins (Herceg et al, 2004a;Herceg et al, 2002;Lelas et al, 2003). Such changed protein structure can cause significant changes in the rheological properties of model systems (Tables 3-6, Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…They are thermo labile (except of proteose peptones), and denaturation of proteins begins at the temperature of 60°C. Denaturation of proteins causes breaking of the hydrogen bridges and disulphide bonds, which assemble secondary and tertiary protein structure (Camire 2002;Herceg et al 2004a). During the process of extrusion in the last section of extruder, before expansion and moulding of finished product, temperatures reach very high levels (up to 150°C).…”
Section: Introductionmentioning
confidence: 99%
“…Improvements in functional properties may be achieved by modifying the protein structure by chemical, enzymatic or physical treatments [11,15,16,18,24,28,37,43]. Functional properties of whey proteins such as emulsification, foaming and gelation are affected by their structure and mainly reflect the functionality of β-lactoglobulin as the most abundant protein, which has the ability to adsorb at the wateroil and air-water interfaces [39].…”
Section: Introductionmentioning
confidence: 99%