Effect of reducing agents on physicochemical properties and gel-forming ability of surimi produced from frozen fish

2004 ◽  
Vol 220 (3-4) ◽  
pp. 316-321 ◽  
Author(s):  
Soottawat Benjakul ◽  
Chutima Thongkaew ◽  
Wonnop Visessanguan
Keyword(s):  
Physicochemical Properties ◽  
Reducing Agents ◽  
Frozen Fish ◽  
Gel Forming Ability

Physicochemical properties and gel-forming ability of surimi from three species of mackerel caught in Southern Thailand

2010 ◽  
Vol 121 (1) ◽  
pp. 85-92 ◽  
Author(s):  
Manat Chaijan ◽  
Worawan Panpipat ◽  
Soottawat Benjakul
Keyword(s):  
Physicochemical Properties ◽  
Southern Thailand ◽  
Gel Forming Ability

scholarly journals An Overview on Collagen and Gelatin-Based Cryogels: Fabrication, Classification, Properties and Biomedical Applications

Polymers ◽  
2021 ◽  
Vol 13 (14) ◽  
pp. 2299
Author(s):  
Yujing He ◽  
Chunhua Wang ◽  
Chenzhi Wang ◽  
Yuanhang Xiao ◽  
Wei Lin
Keyword(s):  
Cell Culture ◽  
Physicochemical Properties ◽  
Biomedical Applications ◽  
Biomedical Application ◽  
Three Dimensional ◽  
Preparation Process ◽  
Precise Characterization ◽  
Gel Forming Ability ◽  
Insight Into

Decades of research into cryogels have resulted in the development of many types of cryogels for various applications. Collagen and gelatin possess nontoxicity, intrinsic gel-forming ability and physicochemical properties, and excellent biocompatibility and biodegradability, making them very desirable candidates for the fabrication of cryogels. Collagen-based cryogels (CBCs) and gelatin-based cryogels (GBCs) have been successfully applied as three-dimensional substrates for cell culture and have shown promise for biomedical use. A key point in the development of CBCs and GBCs is the quantitative and precise characterization of their properties and their correlation with preparation process and parameters, enabling these cryogels to be tuned to match engineering requirements. Great efforts have been devoted to fabricating these types of cryogels and exploring their potential biomedical application. However, to the best of our knowledge, no comprehensive overviews focused on CBCs and GBCs have been reported currently. In this review, we attempt to provide insight into the recent advances on such kinds of cryogels, including their fabrication methods and structural properties, as well as potential biomedical applications.

scholarly journals Effects of the Mixture of Xylooligosaccharides and Egg White Protein on the Physicochemical Properties, Conformation, and Gel-Forming Ability of Culter alburnus Myofibrillar Protein during Multiple Freeze–Thaw Cycles

Foods ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 2007
Author(s):  
Zhongli Zhang ◽  
Zhouyi Xiong ◽  
Noman Walayat ◽  
Jose M. Lorenzo ◽  
Asad Nawaz ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Interaction Force ◽  
Surface Hydrophobicity ◽  
Egg White ◽  
Commercial Application ◽  
Freeze Thaw ◽  
Egg White Protein ◽  
Culter Alburnus ◽  
The Stability ◽  
Gel Forming Ability

This study focuses on the effect of the mixture (XO/EW) of xylooligosaccharides (XO) and egg white protein (EW) on the physicochemical properties, conformation, and gel-forming ability of Culter alburnus myofibrillar proteins (MP) during multiple freeze–thaw (FT) cycles. In our methodology, MP samples added with EW, XO, or XO/EW mixture (1%, v/v) are prepared, and after multiple FT cycles, the XO or XO/EW-treated samples show significant (p < 0.05) inhibition on the decrease of sulfhydryl content and the increase of carbonyl content of MP. Compared with EW, XO or XO/EW could delay the increase of surface hydrophobicity and the decline of secondary and tertiary structural properties of MP, indicating that XO or XO/EW could more effectively increase the stability of MP conformation. Meanwhile, XO/EW could more effectively reduce the decrease of gel strength and gel water holding capacity, and the increase in the T2 relaxation time of MP gel, confirming that XO/EW could substantially improve the MP gel-forming ability. Analysis of intermolecular interaction force proves that, compared with EW, XO/EW could reduce the content decrease of ionic and hydrogen bonds in MP gel. Overall, XO/EW could improve the stability of MP functional properties over multiple FT cycles. This study provides a new perspective for the potential commercial application of EW as a low-calorie cryoprotectant in aquatic products.

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.

Methods for the Concentration of Bovine Ac-Globulin (Factor V)

1961 ◽  
Vol 06 (03) ◽  
pp. 435-444 ◽  
Author(s):  
Ricardo H. Landaburu ◽  
Walter H. Seegers
Keyword(s):  
Room Temperature ◽  
Barium Carbonate ◽  
Deae Cellulose ◽  
Reducing Agents ◽  
Factor V ◽  
Isoelectric Precipitation ◽  
Stabilizing Agent ◽  
Bovine Plasma ◽  
The Stability

SummaryAn attempt was made to obtain Ac-globulin from bovine plasma. The concentrates contain mostly protein, and phosphorus is also present. The stability characteristics vary from one preparation to another, but in general there was no loss before 1 month in a deep freeze or before 1 week in an icebox, or before 5 hours at room temperature. Reducing agents destroy the activity rapidly. S-acetylmercaptosuccinic anhydride is an effective stabilizing agent. Greatest stability was at pH 6.0.In the purification bovine plasma is adsorbed with barium carbonate and diluted 6-fold with water. Protein is removed at pH 6.0 and the Ac-globulin is precipitated at pH 5.0. Rivanol and alcohol fractionation is followed by chromatography on Amberlite IRC-50 or DEAE-cellulose. The final product is obtained by isoelectric precipitation.

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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