Effect of superheated-steam roasting on physicochemical properties of peanut (Arachis hypogea) oil.

Peanut (Arachis hypogaea) is an important source of protein and lipid globally. The effect of superheated-steam roasting on quality of peanut oil was evaluated based on physicochemical quality parameters. Three roasting temperatures (150, 200, and 250 °C) were used for different periods of roasting time and the obtained results were compared with those of conventional roasting. At 250 °C, superheated-steam roasted peanuts yielded more oil (26.84%) than conventionally roasted peanuts (24.85%). Compared with conventional roasting, superheated-steam roasting resulted in lower oil color, peroxide, p-anisidine, free fatty acid, conjugated diene and triene, and acid values and higher viscosity and iodine values in the roasted peanut oil. These values were significantly different from each other (p < 0.05). The fatty acids in roasted peanut oils were affected by roasting temperature and time for both the roasting modes. The superheated steam technique can be used to roast peanuts while maintaining their favorable characteristics.

Assessment of cross-linking in combined cross-linked soy protein isolate gels by microbial transglutaminase and Maillard reaction.

Soy protein isolate (SPI) gels were produced using single cross-linking agents (SCLA) of microbial transglutaminase (MTG) via incubation for 5 or 24 h (SCLA-MTG). When powdered SCLA-MTG gels were heated for 2 h with ribose (R2) (2 g/100 mL), dark brown gels were formed, and these were designated as combined cross-linking agent (CCLA) gels: MTG5(R2) and MTG24(R2). The results showed that the levels of Maillard-derived browning and cross-links of MTG5(R2) and MTG24(R2) gels were significantly (P < 0.05) lower than a control gel produced without MTG (SCLA-R2) even though the percentage of ribose remaining after heating of these gels was similar, indicating that a similar amount of ribose was consumed during heating. epsilon-(gamma-glutamyl)lysine bonds formed during incubation of SPI with MTG may have reduced the free amino group of SPI to take part in the Maillard reaction; nevertheless, ribose took part in the Maillard reaction and initiated the Maillard cross-linkings within the CCLA gels.

Maillard induced complexes of bovine serum albumin--a dilute solution study.

Association of bovine serum albumin (BSA) on heating in the presence and absence of 2% xylose has been studied using dynamic light scattering and sedimentation velocity. When 3% solutions of the protein alone are heated at 95 degrees C association products are formed with molar masses of approximately 2 x 10(6) g/mol, a value which is independent of the time of heating. These aggregates can be dissociated in solvents that disrupt non-covalent bonds. When the reducing sugar xylose is present there is a continuous change in the hydrodynamic properties with time. After 80 min a molar mass in excess of 7 x 10(6) g/mol is obtained. This increase in molar mass is attributed to additional non-disulphide linkages resulting from the Maillard reaction. Information about the gross conformation of the Maillard induced association products has been obtained from MHKS (Mark-Houwink-Kuhn-Sakarada) double logarithmic plots of D20,w and S20,w against molar mass. The values of the MHKS coefficients obtained are most consistent with a linear rod: i.e. the association is of an end-to-end type.