Effect of formulation on physicochemical properties and water status of nutritionally enhanced tortillas

2009 ◽  
Vol 89 (1) ◽  
pp. 73-79 ◽  
Author(s):  
Luca Serventi ◽  
Eleonora Carini ◽  
Elena Curti ◽  
Elena Vittadini
Keyword(s):  
Physicochemical Properties ◽  
Water Status

Effect of Formulation on Physicochemical Properties and Water Status of Nutritionally Enriched Fresh Pasta

2010 ◽  
Vol 5 (5) ◽  
pp. 1642-1652 ◽  
Author(s):  
Eleonora Carini ◽  
Elena Curti ◽  
Elisabetta Spotti ◽  
Elena Vittadini
Keyword(s):  
Physicochemical Properties ◽  
Water Status ◽  
Fresh Pasta

Effect of hydroxypropylmethylcellulose on transition of water status and physicochemical properties of wheat gluten upon frozen storage

2017 ◽  
Vol 63 ◽  
pp. 35-42 ◽  
Author(s):  
Yi-Feng Xuan ◽  
Yuan Zhang ◽  
Yan-Yan Zhao ◽  
Zhi Zheng ◽  
Shao-Tong Jiang ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Water Status ◽  
Wheat Gluten ◽  
Frozen Storage

Effect of different mixers on physicochemical properties and water status of extruded and laminated fresh pasta

2010 ◽  
Vol 122 (2) ◽  
pp. 462-469 ◽  
Author(s):  
Eleonora Carini ◽  
Elena Vittadini ◽  
Elena Curti ◽  
Franco Antoniazzi ◽  
Paola Viazzani
Keyword(s):  
Physicochemical Properties ◽  
Water Status ◽  
Fresh Pasta

Preparation and characterisation of vanadium pentoxide supported rhodium catalyst

1988 ◽  
Vol 46 ◽  
pp. 946-947
Author(s):  
A. Legrouri
Keyword(s):  
Aqueous Solution ◽  
Thermal Decomposition ◽  
Physicochemical Properties ◽  
Surface Area ◽  
Vanadium Pentoxide ◽  
High Purity ◽  
Gas Adsorption ◽  
Rhodium Catalyst ◽  
Optical Methods ◽  
Reducible Oxides

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.

The water status of the roots of soil-grown maize in relation to the maturity of their xylem

1991 ◽  
Vol 82 (2) ◽  
pp. 157-162 ◽  
Author(s):  
X.-L. Wang ◽  
M. J. Canny ◽  
M. E. McCully
Keyword(s):  
Water Status

Studies on the Degradation of Human Fibrinogen by Plasmin and Trypsin

1966 ◽  
Vol 16 (03/04) ◽  
pp. 526-540 ◽  
Author(s):  
E. A Beck ◽  
D. P Jackson
Keyword(s):  
Physicochemical Properties ◽  
Electrophoretic Mobility ◽  
Rapid Loss ◽  
Clotting System ◽  
Human Fibrinogen ◽  
Peptide Bonds ◽  
Physico Chemical ◽  
Starch Gel ◽  
Ph Stat ◽  
Rapid Appearance

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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