Effect of addition of thermally modified cowpea protein on sensory acceptability and textural properties of wheat bread and sponge cake.
This paper investigates the sensory acceptability and textural properties of leavened wheat bread and sponge cake fortified with cow protein isolates that had been denatured and glycated by thermal treatment. Defatted cowpea flour was prepared from cow pea beans and the protein isolate was prepared (CPI) and thermally denatured (DCPI). To prepare glycated cowpea protein isolate (GCPI) the cowpea flour slurry was heat treated before isolation of the protein. CPI was more susceptible to thermal denaturation than GCPI as determined by turbidity and sulphydryl groups resulting in greater loss of solubility. This is attributed to the higher glycation degree and higher carbohydrate content of GCPI as demonstrated by glycoprotein staining of SDS PAGE gels. Water absorption of bread dough was significantly enhanced by DCPI and to a larger extent GCPI compared to the control, resulting in softer texture. CPI resulted in significantly increased crumb hardness in baked bread than the control whereas DCPI or GCPI resulted in significantly softer crumb. Bread fortified with 4% DCPI or GCPI was similar to control as regards sensory and textural properties whereas 4% CPI was significantly different, limiting its inclusion level to 2%. There was a trend for higher sensory acceptability scores for GCPI containing bread compared DCPI. Whole egg was replaced by 20% by GCPI (3.5%) in sponge cake without affecting the sensory acceptability, whereas CPI and DCPI supplemented cakes were significantly different than the control.
Salting-in effect on muscle protein extracted from giant squid (Dosidicus gigas).
The salting-in effect on muscle protein is well-known in food science but hard to explain using conventional theories. Myofibrillar protein extracted from the giant squid (Dosidicus gigas) was selected as a model muscle protein to study this mechanism in KCl solutions. Changes in the secondary structures of myofibrillar protein molecules caused by concentrated salts, particularly in the paramyosin molecule conformation, have been reported. Zeta-potential determinations showed that these secondary structures have modified protein molecule surfaces. The zeta-potential of the myofibrillar protein molecules fell from -7.24±0.82 to -9.99±1.65mV with increasing salt concentration from 0.1 to 0.5M. The corresponding second virial coefficient increased from -85.43±3.8×10(-7) to -3.45±1.3×10(-7) molmLg(-2). The extended law of corresponding states suggests that reduced attractive interactions increase the protein solubility. Solubility measurements in alternating KCl concentrations showed that the conformational change was reversible.
Synergistic Effect of High Temperature and High pH on the Destruction of Salmonella enteritidis and Escherichia co1i O157:H7.
This study was undertaken to determine if high temperature and high pH interact synergistically to enhance the rate of destruction of two important gram-negative foodborne pathogens, Escherichia coli O157:H7 and Salmonella enteritidis . The rates of destruction in NaHCO3-NaOH buffers at pH 7.0, 10.0, and 11.0 were determined at 35, 40, 45, 50, 55, 60, and 65°C. Use of an improved heating protocol eliminated a "tailing effect" at longer exposure times. The present study demonstrated that the combination of high pH and high temperature resulted in a highly significant synergistic interaction (P > F = 0.0001), which caused rapid death of both E. coli O157:H7 and S. enteritidis . This "alka-therm" technology might be used commercially to destroy gram-negative foodborne pathogens on various raw agricultural commodities.