scholarly journals Physicochemical properties analysis of bamboo salt on chicken emulsion sausage

2020 ◽  
Vol 62 (1) ◽  
pp. 103-110
Author(s):  
Sol-Hee Lee ◽  
Gye-Woong Kim ◽  
Hack-Youn Kim
Food Research ◽  
2021 ◽  
Vol 5 (3) ◽  
pp. 225-235
Author(s):  
M. Hamzah ◽  
M.I. Shaik ◽  
N.,M. Sarbon

The present study aimed to investigate the effect of silver catfish (Pangasius sp.) protein hydrolysate (SCPH) on physicochemical properties and oxidative stability of emulsion sausage prepared from shortfin scad (Decapterus macrosoma). The SCPH with different concentrations (1, 2, and 3%) was added into fish emulsion sausage followed by characterization of its physicochemical properties. The results obtained from this study revealed that the fish emulsion sausages contain high moisture content (63.49-66.85%), protein content (18.04-21.89%), fat content (7.16-8.59%), carbohydrate content (2.28- 2.72%) and low ash contents (1.83-2.17%). The addition of SCPH improvised the hardness, cohesiveness, chewiness and resilience of the emulsion sausage (p<0.05) compared to the control sample. The finer fat globules were visualized in the sample added with SCPH at higher concentration of 3% (10-20 µm) compared to other concentrations (1 and 2%). Besides, the incorporation of SCPH at all concentrations shows a significant difference on L*, a* and b* values of the emulsion sausages during extended storage of 12 days (p<0.05). The SCPH was shown to retard lipid oxidation of sausage after extended storage of 12 days, with lower PV and TBARS values. Therefore, the effectiveness in retarding lipid oxidation achieved with the higher concentration of SCPH and it also capable to retain textural properties of fish emulsion sausage in the refrigerated storage of 12 days. Thus, as an alternative antioxidant in fish emulsion sausage, SCPH showed a potential to be used as it improved the physicochemical properties and oxidative stability of fish emulsion sausage.


Meat Science ◽  
2010 ◽  
Vol 86 (4) ◽  
pp. 960-965 ◽  
Author(s):  
Hack-Youn Kim ◽  
Eui-Soo Lee ◽  
Jong-Youn Jeong ◽  
Ji-Hun Choi ◽  
Yun-Sang Choi ◽  
...  

Food Research ◽  
2021 ◽  
Vol 5 (4) ◽  
pp. 248-258
Author(s):  
N.A. Halmi ◽  
N.M. Sarbon ◽  
N.M. Sarbon

The aim of this study was to identify the physicochemical properties, oxidative stability and sensory acceptability of shortfin scad (Decapterus macrosoma) emulsion sausage incorporated with commercial surimi and silver catfish (Pengasius) protein hydrolysate. Fish emulsion sausage was prepared with fish mince and surimi ratios as follows: Formulation A (100:0); B (60:40); C (40:60); D (0:100). The proximate compositions of the fish emulsion sausages were determined. An increase in surimi percentage was increased lightness (L*) and decreased redness (a*) values of the sausages significantly (p<0.05). The higher fish mince ratio caused an increase in texture profile and a betteremulsified microstructure with fewer voids compared to the control. The fish protein hydrolysate could help maintain oxidative stability, as it has antioxidant properties. Moreover, the sensory evaluation indicated that all formulations of shortfin scad sausage incorporated with surimi and fish protein hydrolysate can be accepted by consumers, with formulation B had the highest rank as compared to control (100% surimi).


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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