Effects of buttermilk powders on emulsification properties and acid tolerance of cream.

Unlabelled: Emulsifying properties and acid tolerance are 2 of the most important characteristics of cream. The effects of the buttermilk component, especially its phospholipids, on the emulsifying properties and acid tolerance of cream were investigated in this study. Two buttermilks with differing phospholipid contents and skimmed milk were used to evaluate the effects of phospholipids on the aforementioned parameters.

Dynamic surface tension and surface dilatational elasticity properties of mixed surfactant/protein systems.

We present the study on dynamic surface tension and surface dilatational elasticity properties of dilute aqueous systems of pentaglycerol fatty acid esters (pentaglycerol monostearate, C18G5, and pentaglycerol monooleate, C18:1G5, whey protein, sodium caseinate, and mixed surfactant and protein at room temperature. The adsorption kinetics at the air-liquid interface has been studied by bubble pressure tensiometer and the oscillation bubble (rising drop) method. It has been shown that the dynamic surface tension curve basically presents two-regions; namely induction region and rapid fall region.

Aqueous foam stabilized by dispersed surfactant solid and lamellar liquid crystalline phase.

Foaming properties of dilute aqueous solutions of pentaglycerol monostearate (C(18)G(5)) and pentaglycerol monooleate (C(18:1)G(5)) have been studied at 25 degrees C. The aqueous C(18)G(5) system formed highly persistent foams, which did not rupture for several days. Foamability and foam stability were increased on increasing the surfactant concentration in both C(18)G(5) and C(18:1)G(5) systems.

Hyper-processive and slower DNA chain elongation catalysed by DNA polymerase III holoenzyme purified from the dnaE173 mutator mutant of Escherichia coli.

Background: A strong mutator mutation, dnaE173, leads to a Glu612 --> Lys amino acid change in the alpha subunit of Escherichia coli DNA polymerase III (PolIII) holoenzyme and abolishes the proofreading function of the replicative enzyme without affecting the 3' --> 5' exonuclease activity of the epsilon subunit. The dnaE173 mutator is unique in its ability to induce sequence-substitution mutations, suggesting that an unknown function of the alpha subunit is hampered by the dnaE173 mutation.

Results: A PolIII holoenzyme reconstituted from dnaE173 PolIII* (DNA polymerase III holoenzyme lacking the beta clamp subunit) and the beta subunit showed a strong resistance to replication-pausing on the template DNA and readily promoted strand-displacement DNA synthesis.