Tyre C. Lanier

Chicken plasma protein affects gelation of surimi from bigeye snapper (Priacanthus tayenus)

Effect of chicken plasma protein (CPP) at different concentrations on gel properties of grade SA and A bigeye snapper surimi was investigated. Addition of 0.5% CPP in combination with setting at 40 °C for 30 min prior to heating at 90 °C for 20 min resulted in the highest breaking force and deformation (P<0.05). However, whiteness decreased to some extent. CPP was able to prevent the degradation of surimi proteins as indicated by the decrease in TCA-soluble peptides (P<0.05). Electrophoretic studies revealed that myosin heavy chain underwent polymerization to a lower extent as CPP concentration increased. Therefore, CPP worked as protease inhibitor rather than protein cross-linker. Microstructure of kamaboko gels, added with 0.5% CPP, had less linkage between protein strands with a coarser fibrillar structure, indicating the interfering effect of CPP on cross-linking of myofibrillar proteins. Thus, at an appropriate amount, CPP possibly worked as a filler in the surimi gel matrix, resulting in gel strengthening.

Capillary Pressure as Related to Water Holding in Polyacrylamide and Chicken Protein Gels

UNLABELLED The ability of food gels to hold water affects product yield and organoleptic quality. Most researchers believe that water is held by capillarity such that gels having smaller mean pore diameter and a more hydrophilic surface hold water more tightly. To date, however, only qualitative evidence relating pore size to water holding (WH) properties has been provided. The present study sought to provide quantitative confirmation of this hypothesis. Scanning electron microscopy coupled with image analysis was used to measure pore size, and water contact angle with the gel surface was measured by the captive bubble method, in both model polyacrylamide gels and heat-induced protein (minced chicken breast) gels. These were related to water lost during cooking of meat pastes to form gels (cooking loss (CL)), as well as water lost upon centrifugation (expressible water (EW)) or by capillary suction (CSL) of all prepared gels, as inverse measures of WH. As predicted by the Young-Laplace equation for calculating capillary pressure, the presumed mechanism of WH, gels with lower water losses exhibited a more hydrophilic surface (smaller contact angle). Yet, both lower CL and CSL correlated with larger mean pore diameter of gels, not smaller as had been expected. Polyacrylamide gels varied more in WH than did prepared meat gels, yet only the capillary suction method was sensitive enough to detect these differences. PRACTICAL APPLICATION  The ability of gels to hold water is important for economics of processing, food quality, and food safety. This study investigated the prevailing theory for how gels hold water, capillarity. Both the pore sizes of gel microstructures and the degree of hydrophilicity of the polymers comprising each gel were quantitatively assessed and related to water holding (WH) properties, and this was the first report using such methodologies. It appeared that the degree of hydrophilicity was much more important explaining WH properties than pore size, and that future research of this kind should be carried out.

Cryoprotectants for Improving Frozen-Food Quality

Cryoprotectants are compounds that improve the quality and extend the shelf life of frozen foods. The term cryoprotectant includes all compounds that help to prevent deleterious changes in foods caused by freezing and thawing processes or frozen storage. These substances may be added during processing and product formulation or produced naturally in the living organism from which the food is derived.

Rapid Heating of Alaska Pollock and Chicken Breast Myofibrillar Protein Gels as Affecting Water-Holding Properties

The gelation response of salted muscle minces to rapid versus slow heating rates is thought to differ between homeotherm and poikilotherm species. This study investigated water-holding (WH) properties of pastes prepared from refined myofibrils, at equal pH, of chicken breast versus Alaska pollock both during [cook loss (CL)] and following [expressible water (EW)] their cooking by rapid [microwave (MW)] versus slow [water bath (WB)] heating and whether such properties were related to gel matrix structure parameters and water mobility. Results did not confirm the industrial experience that pastes of meat from homeotherms benefit from slower cooking. Gels of equally high WH ability (low CL or EW) were made by rapid heating when the holding time did not exceed 5 min prior to cooling, which was sufficient for completion of gelation. Reduced CL and EW correlated with larger and smaller amplitudes of T21 and T22 water pools, respectively, measured by time-domain nuclear magnetic resonance (TD-NMR).

Effects of heating rate and pH on fracture and water-holding properties of globular protein gels as explained by micro-phase separation.

UNLABELLED The effect of heating rate and pH on fracture properties and held water (HW) of globular protein gels was investigated. The study was divided into 2 experiments. In the 1st experiment, whey protein isolate (WPI) and egg white protein (EWP) gels were formed at pH 4.5 and 7.0 using heating rates ranging from 0.1 to 35 °C/min and holding times at 80 °C up to 240 min. The 2nd experiment used one heating condition (80 °C for 60 min) and probed in detail the pH range of 4.5 to 7.0 for EWP gels. Fracture properties of gels were measured by torsional deformation and HW was measured as the amount of fluid retained after a mild centrifugation. Single or micro-phase separated conditions were determined by confocal laser scanning microscopy. The effect of heating rate on fracture properties and HW of globular protein gels can be explained by phase stability of the protein dispersion and total thermal input. Minimal difference in fracture properties and HW of EWP gels at pH 4.5 compared with pH 7.0 were observed while WPI gels were stronger and had higher HW at pH 7.0 as compared to 4.5. This was due to a mild degree of micro-phase separation of EWP gels across the pH range whereas WPI gels only showed an extreme micro-phase separation in a narrow pH range. In summary, gel formation and physical properties of globular protein gels can be explained by micro-phase separation. PRACTICAL APPLICATION The effect of heating conditions on hardness and water-holding properties of protein gels is explained by the relative percentage of micro-phase separated proteins. Heating rates that are too rapid require additional holding time at the end-point temperature to allow for full network development. Increase in degree of micro-phase separation decreases the ability for protein gels to hold water.

Capillarity proposed as the predominant mechanism of water and fat stabilization in cooked comminuted meat batters.

Fat- and nonfat-containing meat gels structurally became coarser and porous by partial substitution of whey protein isolate for myofibrillar protein, creating a weaker texture plus greater cook loss (CL: fat+water) and expressible water (EW). Microstructure examinations revealed a tendency for fat to coalesce during cooking of the more coarse-structured gels. This tendency was unaffected by fat pre-emulsification prior to addition, arguing against a strong role of an interfacial protein film in stabilizing fat. Instead, a gel structure with evenly distributed small pores leads to lower CL and EW, thus controlling both water- and fat- holding since fat cannot readily permeate small water-filled hydrophilic pores. Only when large pores or continuous fissures are structurally present can water be released, allowing liquid fat to also migrate and coalesce. This changes the current paradigm of understanding regarding the mechanism of fat/water-holding in comminuted meat products: gel capillarity (gel structure), not fat emulsifying ability of protein, is the likely determining factor.

Diffusion of active proteins into fish meat to minimize proteolytic degradation.

Proteases in fish muscle often cause undesired softening of intact meat pieces during refrigerated storage or slow cooking. Several food-grade proteinaceous inhibitors can overcome this softening if properly delivered to the intracellular sites where proteases are located. Fluorescence recovery after photobleaching (FRAP) and laser scanning confocal microscopy (LSCM) were used to measure the translational diffusion of fluorescein isothiocyanate (FITC)-labeled protease inhibitors into intact muscle fibers of halibut. Diffusion coefficients (D) of alpha-2-macroglobulin (720 kDa), soybean trypsin inhibitor (21 kDa), and cystatin (12 kDa) were measured in both muscle fibers and dilute aqueous solutions. On the time scale of the observation (35 min), cystatin and soybean trypsin inhibitor diffused through the cell membrane (sarcolemma) and sarcoplasm, but at a considerably slower rate (>10-fold difference) than in dilute aqueous solution. alpha-2-Macroglobulin did not diffuse into muscle cells within the time frame of the experiment, but did completely penetrate the cell during overnight exposure. The present study thus shows a clear dependence of D on protein inhibitor size when moving within intact skeletal muscle fibers. Low molecular weight protease inhibitors such as cystatin can be effectively diffused into intact fish muscle cells to minimize proteolytic activity and meat softening.

Simultaneous application of microbial transglutaminase and high hydrostatic pressure to improve heat induced gelation of pork plasma.

The effects of treating porcine plasma with microbial tranglutaminase (MTGase) under high hydrostatic pressure (HHP) were studied as a means of improving its gel-forming properties when subsequently heated at pH 5.5, near the pH of meats. Plasma containing varying levels of commercial MTGase was pressurized (400MPa, room temperature, pH 7) for different times, and adjusted to pH 5.5 prior to heating to induce gelation. MTGase-treatment under HHP led to greater enhancement of heat-induced plasma gel properties as compared to control samples. The greatest improvements were achieved by pressurising plasma with 43.3U MTGase/g protein for 30min, thereby achieving recoveries of 49% and 63% in fracture force (gel strength) and fracture distance (gel deformability) of the subsequently heat-induced gels, respectively, relative to gel properties obtained by heating untreated plasma at physiological conditions (pH 7.5).

Rheological and Textural Properties of Pacific Whiting Surimi Gels As Influenced by Chicken Plasma

Rheological properties of Pacific whiting surimi, in the absence and presence of chicken plasma (CP) at different levels (0.3–3.0%, w/w), were studied by dynamic rheological (small strain) and torsion fracture measurements, respectively. The surimi paste exhibited two major distinctive rheological transitions during heating (1°C/min) from 20 to 90°C with peaks observed at 33 and 56°C. The abrupt loss of G′ upon heating from 47 to 57°C, and the occurrence of small peak of phase angle at the same temperature range were prevented by the addition of CP. Nevertheless, the final G′ of the surimi paste added with CP was lower than that of the control. But shear fracture stress of both kamaboko and modori gels increased as the CP levels increased and shear strain increased with the addition of CP up to 2% (P < 0.05). CP inhibited the degradation of myosin heavy chains (MHC) caused by endogenous proteinases as indicated by more retained MHC and lowered TCA-soluble peptide content. Whiteness of gels decreased somewhat with increasing CP levels. CP, thus, could be a helpful additive for improving gelling properties of Pacific whiting surimi

Rapid Heating of Alaska Pollock and Chicken Breast Myofibrillar Proteins as Affecting Gel Rheological Properties

Surimi seafoods (fish/poikilotherm protein) in the U.S.A. are typically cooked rapidly to 90+°C, while comminuted products made from land animals (meat/homeotherm protein) are purposely cooked much more slowly, and to lower endpoint temperatures (near 70 °C). We studied heating rate (0.5, 25, or 90 °C/min) and endpoint temperature (45 to 90 °C) effects on rheological properties (fracture, small strain) of washed myofibril gels derived from fish (Alaska pollock) compared with chicken breast at a common pH (6.75). This was contrasted with published data on gelation kinetics of chicken myosin over the same temperature range. Heating rate had no effect on fracture properties of fish gels but slow heating did yield somewhat stronger, but not more deformable, chicken gels. Maximum gel strength by rapid heating could be achieved within 5 min holding after less than 1 min heating time. Dynamic testing by small strain revealed poor correspondence of the present data to that published for gelling response of chicken breast myosin in the same temperature range. The common practice of reporting small-strain rheological parameters measured at the endpoint temperature was also shown to be misleading, since upon cooling, there was much less difference in rigidity between rapidly and slowly heated gels for either species.