pectins has been researched along with tartaric-acid* in 2 studies
2 other study(ies) available for pectins and tartaric-acid
| Article | Year |
|---|---|
Structure formation in sugar containing pectin gels - influence of tartaric acid content (pH) and cooling rate on the gelation of high-methoxylated pectin.
The aim of the study was the application of a recently published method, using structuring parameters calculated from dG'/dt, for the characterisation of the pectin sugar acid gelation process. The influence of cooling rate and pH on structure formation of HM pectin gels containing 65 wt.% sucrose were investigated. The results show that the structure formation process as well as the properties of the final gels strongly depended on both parameters. With increasing cooling rates from 0.5 to 1.0 K/min the initial structuring temperature slightly decreased and the maximum structuring velocity increased. The lower the cooling rates, the firmer and more elastic were the final gels. With increasing acid content (decreasing pH from 2.5-2.0) the initial structuring temperatures were nearly constant. The final gel properties varied visibly but not systematically. Gels with the lowest and highest pH were less elastic and weaker compared to those with medium acid concentrations. Topics: Gels; Hydrogen-Ion Concentration; Molecular Structure; Pectins; Rheology; Tartrates; Temperature | 2014 |
Flow calorimetry--a useful tool for determination of immobilized cis-epoxysuccinate hydrolase activity from Nocardia tartaricans.
Bacterial cells Nocardia tartaricans with cis-epoxysuccinate hydrolase activity were entrapped in hardened calcium pectate gel by a commercial high performance encapsulator. This enzyme (in a single step reaction with no formation of side products) was used to hydrolyze disodium cis-epoxysuccinate to a pure enantiomer--disodium L-(+)-tartrate. Activities of this enzyme were determined using flow calorimetry. The validity of this method was corroborated by HPLC and isotachophoresis. The immobilized biocatalyst has activity (75.8 U/mgdry) able to convert disodium cis-epoxysuccinate to disodium tartrate at 94% yield in 5.5h. Immobilization of N. tartaricans in hardened calcium pectate gel beads had a positive effect on the activity of cis-epoxysuccinate hydrolase, storage stability, yield, and time of bioconversion. Topics: Calorimetry; Enzyme Stability; Enzymes, Immobilized; Hydrolases; Kinetics; Microspheres; Nocardiaceae; Pectins; Succinates; Tartrates | 2004 |