Diamond-like carbon films were prepared by high intensity pulsed ion beam ablation of graphite targets. A 350 keV, 35 kA, 400 ns pulse width beam, consisting primarily of carbon ions and protons, was focused onto a graphite target at a fluence of 15-45 J/cm2. Films were deposited onto substrates positioned in an angular array from normal to the target to 90° off normal. Deposition rates up to 30 nm per pulse, corresponding to an instantaneous deposition rate greater than 1 mm/sec, have been observed. Electrical resistivities between 1 and 1000 ohm·cm were measured for these films. XRD scans showed that no crystalline structure developed in the films. SEM revealed that the bulk of the films contain material with feature sizes on the order of 100 nm, but micron size particles were deposited as well. Both Raman and electron energy loss spectroscopy indicated significant amounts of sp3 bonded carbon present in most of the films.

Acid-set milk gels containing up to 30 mM added hexametaphosphate, oxalate, citrate, EDTA or orthophosphate were prepared using gluconic acid-δ-lactone and their properties investigated. Increases in the apparent shear modulus were observed in the gels containing hexametaphosphate, oxalate, citrate and EDTA. The effect was maximum for hexametaphosphate-containing gels at ˜ 8 mM. Increases were also observed in the force required to break the gels, and for added hexametaphosphate the effect peaked at ˜ 5 niM. The ability of the gels to resist syneresis was investigated by a cut, tip and drain type test and by a centrifugation method. In both tests, resistance to syneresis was increased by added hexametaphosphate, oxalate, citrate and EDTA. The additions of anions were shown to cause disintegration of the micelles and release caseins to the serum. It is suggested that the improved homogeneity of casein distribution that results allows greater opportunity for protein-protein interaction during gel formation and leads to improved properties. Controlled micelle disintegration would therefore appear to offer promise for the development of improved or novel products.

A general theory of gel formation by cross-linking of polymer molecules, orginally developed for the study of rubber vulcanization, is proposed as a model for milk gel formation. The model divides gel formation and development into 4 stages, an enzymic and a non-enzymic stage preceding gelation, then a stage of material transition from the sol to the gelled state and a stage of increase in gel strength due to internal cross-link formations. The 2 post-gelation stages overlap to a variable degree depending upon particular circumstances. Gel formation and properties are interpreted in terms of the number of initial units which combine to form the gel and the number of cross-links eventually formed by each unit. When combined with a kinetic expression for the rate of cross-link formation the time course of gel shear modulus development or of the incorporation of material into the gel may be predicted. The classical asymmetric sigmoid shape of gel shear modulus development curves results from the third stage of material transition into the gel, which in turn depends upon the number of cross-links eventually formed by each initial unit. The modulus of mature gels is found to depend upon the square of material concentration, and gel breaking strength is found to be proportional to the modulus, in agreement with the predictions of the theory.

The effects of thermization (a sub-pasteurization heat treatment), followed by cold storage at 7 °C for up to 3 d on the post-gelation behaviour of rennet-induced gels from alternate-day collected milks, pasteurized before testing, were investigated. Observations of the time course of gel rigidity modulus development and of the syneresis of cut curds were fitted to a general exponential relationship to aid interpretation. Milk performance was assessed by measurements of rennet coagulation time at pH 6·5, various gel rigidity and syneresis parameters and losses of protein and Ca to the whey. A small but significant reduction in protein losses to the whey (mean 0·05%) was the only effect resulting from thermization. Cold storage gave rise to significantly weaker gels than those from unstored controls. The gels from cold-stored milks attained 50% of their maximum rigidity modulus in significantly less time and lost significantly more protein (mean 0·11%) to the whey. Samples cold stored for 1, 2 or 3 d were not significantly different from each other and no other parameters were affected. No significant interactions between thermization and cold storage were found.