Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
Food Chem ; 196: 769-75, 2016 Apr 01.
Article in English | MEDLINE | ID: mdl-26593553

ABSTRACT

Conformational and thermal-rheological properties of acidic (APC) and neutral (NPC) protein concentrates were evaluated and compared to those of squid (Dosidicus gigas) muscle proteins (SM). Surface hydrophobicity, sulfhydryl status, secondary structure profile, differential scanning calorimetry and oscillatory dynamic rheology were used to evaluate the effect of treatments on protein properties. Acidic condition during the washing process (APC) promoted structural and conformational changes in the protein present in the concentrate produced. These changes were enhanced during the heat setting of the corresponding sol. Results demonstrate that washing squid muscle under the proposed acidic conditions is a feasible technological alternative for squid-based surimi production improving its yield and gel-forming ability.


Subject(s)
Decapodiformes/chemistry , Food Handling/methods , Muscle Proteins/chemistry , Seafood/analysis , Animals , Calorimetry, Differential Scanning , Hydrogen-Ion Concentration , Muscles/chemistry , Rheology
2.
Food Chem ; 110(2): 486-92, 2008 Sep 15.
Article in English | MEDLINE | ID: mdl-26049243

ABSTRACT

A protein concentrate from giant squid (Dosidicus gigas) was produced under acidic conditions and its functional-technological capability evaluated in terms of its gel-forming ability, water holding capacity and colour attributes. Technological functionality of the concentrate was compared with that of squid muscle and a neutral concentrate. Protein-protein aggregates insoluble at high ionic strength (I=0.5M), were detected in the acidic concentrate as result of processing with no preclusion of its gel-forming ability during the sol-to-gel thermal transition. Even though washing under acidic condition promoted autolysis of the myosin heavy chain, the acidic concentrate displayed an outstanding ability to gel giving samples with a gel strength of 455 and 1160gcm at 75% and 90% compression respectively, and an AA folding test grade indicative of high gel strength, elasticity, and cohesiveness. The process proved to be a good alternative for obtaining a functional protein concentrate from giant squid muscle.

SELECTION OF CITATIONS
SEARCH DETAIL
...