The Effect of Enzymatic Alcoholysis on the Physicochemical Properties of Commercial Cocoa Butter Substitutes

2011 ◽  
Vol 10 (8) ◽  
pp. 718-723 ◽  
Author(s):  
R. Nazaruddin ◽  
S. Nurul i Zakiyan ◽  
S. Mamot
Author(s):  
Larissa M. Grimaldi ◽  
◽  
Kamila R. Rodrigues de Godoi ◽  
Fernanda L. Lüdtke ◽  
Thais J. Silva ◽  
...  

Babassu and murumuru palms are both sources of lauric acid. Due to their high oxidative stability and well-defined melting points, fats from both plants are widely used in the cosmetic industry and in the preparation of specialty fats for confectionery, ice cream, margarines, and cocoa butter substitutes. This article reviews the composition and physicochemical properties of these exotic fats.


2012 ◽  
Vol 63 (1) ◽  
pp. 89-99 ◽  
Author(s):  
A. P. B. Ribeiro ◽  
R. Corrêa Basso ◽  
L. A.G. Gonçalves ◽  
L. A. Gioielli ◽  
A. Oliveira dos Santos ◽  
...  

LWT ◽  
2021 ◽  
pp. 112556
Author(s):  
Norazlina M.R ◽  
Jahurul M.H.A ◽  
Hasmadi M ◽  
Mansoor A.H ◽  
Patricia M ◽  
...  

Author(s):  
A. Legrouri

The industrial importance of metal catalysts supported on reducible oxides has stimulated considerable interest during the last few years. This presentation reports on the study of the physicochemical properties of metallic rhodium supported on vanadium pentoxide (Rh/V2O5). Electron optical methods, in conjunction with other techniques, were used to characterise the catalyst before its use in the hydrogenolysis of butane; a reaction for which Rh metal is known to be among the most active catalysts.V2O5 powder was prepared by thermal decomposition of high purity ammonium metavanadate in air at 400 °C for 2 hours. Previous studies of the microstructure of this compound, by HREM, SEM and gas adsorption, showed it to be non— porous with a very low surface area of 6m2/g3. The metal loading of the catalyst used was lwt%Rh on V2Q5. It was prepared by wet impregnating the support with an aqueous solution of RhCI3.3H2O.


1966 ◽  
Vol 16 (03/04) ◽  
pp. 526-540 ◽  
Author(s):  
E. A Beck ◽  
D. P Jackson

SummaryThe effects of trypsin and plasmin on the functional and physicochemical properties of purified human fibrinogen were observed at various stages of proteolysis. Concentrations of plasmin and trypsin that produced fibrinogenolysis at comparable rates as measured in a pH stat produced, at similar rates, loss of precipitability of fibrinogen by heat and ammonium sulphate and alterations in electrophoretic mobility on starch gel. Trypsin produced a more rapid loss of clottability of fibrinogen and a more rapid appearance of inhibitors of the thrombin-fibrinogen clotting system than did plasmin. Consistent differences were noted between the effects of trypsin and plasmin on the immunoelectrophoretic properties of fibrinogen during the early stages of proteolysis.These results are consistent with the hypothesis that trypsin initially reacts with the same peptide bonds of fibrinogen that are split by thrombin, but these same bonds do not appear to be split initially by plasmin. Measurement of the various functional and physico-chemical changes produced by the action of trypsin and plasmin on fibrinogen can be used to recognize various stages of proteolysis.


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