EFFECTS OF CHITOSAN ON GELLING PROPERTIES OF LOW QUALITY SURIMI

In order to produce a strong and elastic gel from low quality walleye pollock surimi, use of chitosan was examined. The strength of gels was nearly doubled by the addition of 1.5% chitosan when salted surimi pastes were set below 25C. In contrast, chitin did not cause any changes in the physical texture of gels. When salted surimi pastes containing 1.5% chitosan were set at 20C, a large decrease in the proportion of myosin heavy chain was observed with a concomitant increase in components with molecular weights heavier than myosin heavy chain. Since the addition of EGTA, an inhibitor of transglutaminase, to surimi reduced gel strength and minimized myosin heavy chain polymerization, it is suggested that the enhancing effect ofchitosan on the gel formation of walleye pollock surimi could be due to the activity of the endogenous transglutaminase known to be present in this surimi.     

大豆蛋白凝固机理

综述了国内外在关于大豆蛋白胶凝方面所取得的研究进展，主要包括热胶凝、盐胶凝、酸胶凝以及酶胶凝等的机理。     

COLD GELATION OF WHEY PROTEIN EMULSIONS

Stable and homogeneous emulsion‐filled gels were prepared by cold gelation of whey protein isolate (WPI) emulsions. A suspension of heat‐denatured WPI (soluble WPI aggregates) was mixed with a 40% (w/w) oil‐in‐water emulsion to obtain gels with varying concentrations of WPI aggregates and oil. For emulsions stabilized with native WPI, creaming was observed upon mixing of the emulsion with a suspension of WPI aggregates, likely as a result of depletion flocculation induced by the differences in size between the droplets and aggregates. For emulsions stabilized with soluble WPI aggregates, the obtained filled suspension was stable against creaming, and homogeneous emulsion‐filled gels with varying protein and oil concentrations were obtained. Large deformation properties of the emulsion‐filled cold‐set WPI gels were determined by uniaxial compression. With increasing oil concentration, the fracture stress increases slightly, whereas the fracture strain decreases slightly. Small deformation properties were determined by oscillatory rheology. The storage modulus after 16 h of acidification was taken as a measure of the gel stiffness. Experimental results were in good agreement with predictions according to van der Poel's theory for the effect of oil concentration on the stiffness of filled gels. Especially, the influence of the modulus of the matrix on the effect of the oil droplets was in good agreement with van der Poel's theory.     

NUTRITIONAL QUALITY OF SURIMI POWDER FROM THREADFIN BREAM

Threadfin bream (Nemipterus japonicus) surimi was dried to produce surimi powder with a moisture content of about 5%. The surimi powder contained 72% protein and 20% carbohydrate. Although the protein content was lower than for dried fish flesh, the nutritional quality of surimi powder was higher than for dried fish flesh and casein. The protein efficiency ratio (PER), net protein ratio (NPR), apparent digestibility and true digestibility of surimi powder were 3.42, 5.37, 92.1 and 95.3, respectively, while for fish flesh they were 3.21, 5.20, 90.7 and 94.4, respectively. Freeze-dried surimi powder had superior nutritional properties compared to oven-dried method.     

INFLUENCE OF TRANSGLUTAMINASE-INDUCED CROSS-LINKING ON IN VITRO DIGESTIBILITY OF SOY PROTEIN ISOLATE

The influence of covalent cross‐linking by microbial transglutaminase (MTGase) on the sequential in vitro pepsin and trypsin digestion process and the digestibility of soy protein isolate (SPI), was investigated by sodium dodecylsulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) and nitrogen release analyses. Various subunits of β‐conglycinin and acidic subunits of glycinin were cross‐linked by MTGase to form high molecular weight (MW) biopolymers, while basic subunits of glycinin were unaffected. SDS‐PAGE analysis indicated that the cross‐linking mainly affected in vitro pepsin digestion pattern of various subunits of β‐conglycinin, while the trypsin digestion pattern of native SPI was nearly unaffected. Nitrogen release analysis showed that the in vitro pepsin or/and trypsin digestibility of native SPI (at the end of pepsin or trypsin ingestion) was significantly decreased (P ≤ 0.01) by the MTGase treatment (for more than 2 h). The cross‐linking by MTGase also significantly decreased the in vitro digestibility of preheated SPI. These results suggest that the cross‐linking by means of transglutaminase may negatively affect the nutritional properties of food proteins.     

CHARACTERIZATION OF PROTEINASE RECOVERED FROM PACIFIC WHITING SURIMI WASH WATER

Pacific whiting surimi wash water (SWW) proteinase was recovered by ohmic heating, ultrafiltration, and freeze-drying. By these processes, 5.9-fold purification was achieved. The most efficient step was ohmic heating, which concentrated the proteinase by 4.8 fold. Specific activity of the recovered SWW proteinase on casein and Z-Phe-Arg-NMec was 28.2 and 0.17 U/mg protein, respectively. The SWW proteinase showed good hydrolytic activity towards casein, acid-denatured hemoglobin and myofibrils. Acidification increased specific activity on all substrates tested but reduced thermal stability. β-Mercaptoethanol, dithiothreitol and urea enhanced activity against Z-Phe-Arg-NMec. Proteinase activity on Z-Phe-Arg-NMec showed an optimum pH of 4.0. The recovered proteinase showed 18.5% residual activity after 7 week storage at 4C.     

RECOVERY OF PROTEINASE FROM PACIFIC WHITING SURIMI WASH WATER

A proteinase from Pacific whiting surimi wash water (SWW) was recovered by ohmic heating, ultrafiltration, and freeze drying with overall yield of 0.83 g protein/L SWW and 78% recovery of activity. Ohmic heating conditions were optimized for the maximum recovery of the enzyme. Different applied voltages (50, 70, 90 V) showed no differences in efficiency for removing protein and retaining cathepsin Lactivity. Cathepsin L activity reached its maximum after ohmic heating to 55C whereas cathepsin B activity decreased constantly with increased temperature. A constant reduction in protein content was observed with the increase in temperatures from 45C to 60C and holding time up to 5 min. The highest retention of both total and specific activity of cathepsin L was obtained with the treatment at 55C for 3 min. Under these conditions, 193% activity was recovered from SWW although a large amount of the activity was lost by the subsequent steps of ultrafiltration and freeze drying.     

HEAT-INDUCED GELATION AND PROTEIN-PROTEIN INTERACTION OF ACTOMYOSIN1

Natural actomyosin (NAM) and “crude” actomyosin formed gels yielding maximum strengths (from back extrusion force) at pH 5.0 and 5.5, respectively. At pH 6.0, NAM gels had a least protein concentration endpoint (LCE) value of 6 mg/ml. Gel strength increased exponentially with an increase of NAM concentration from 3.75–10 mg/ml. With constant time (30 min)-temperature heating, NAM gel forces increased by 20.5% (NS, P>0.05) in the 30–80°C range. Arrhenius plots of NAM interaction in solution and in gelation at pH 6.0 indicated two different reaction mechanisms within the temperature zones above and below approximately 35°C for solutions and 40°C for gels. Similarity of interaction slopes above the 35–40°C region suggested one reaction mechanism for NAM molecular aggregation in solution and gelation.     

TEXTURE DEGRADATION KINETICS OF GELS MADE FROM PACIFIC WHITING SURIMI

Degradation kinetics of whiting surimi gel texture were examined over a temperature/time range (40–85C, 0.5–35 min). Changes in textural properties of whiting surimi gel were mainly affected by proteolytic activity of endogenous proteinase. A decrease of failure shear stress and shear strain followed first order kinetics. The kinetic parameters developed using either isothermal or nonisothermal principles were similar. Degradation rate of gel texture increased with temperature, reaching a maximum at 55C. It then decreased to a minimum at 70C. E_a values for the activation and inactivation temperature range were 138.6–162.6 and 13.5–35.0 kJ/mol, respectively.     

壳聚糖用作纸浆增干强的研究

壳聚糖用作纸张干增强剂已有较多的报道,但其粘度和脱乙酰度的大小对纸张增强效果影响的研究尚属空白。本文以漂白针叶木硫酸盐浆为原料,对较宽粘度范围和脱乙酰度范围的壳聚糖样品进行了筛选。以对木浆的增强效果为标准,从中选出了几种增强效果较好的样品,为壳聚糖的进一步改性奠定了基础。     

ɛ-POLYLYSINE IMPROVES THE QUALITY OF SURIMI PRODUCTS

To apply ɛ-polylysine (PL) as a natural food preservative for the preparation of surimi products, effects of added PL on the textural properties and shelf-life of kamaboko gels were investigated. Kamaboko gels were prepared by setting at 30C for 1 h, then heating at 80C for 20 min. Breaking force and breaking strain of kamaboko gels increased slightly with increasing PL concentration up to 0.2% and decreased at 0.4%. However, the protein subunit component composition of kamaboko gels did not vary with the amount of PL added, indicating that PL did not promote the polymerization of myosin heavy chain. The increased pH value of surimi to around 7.6 as the result of the incorporation of 0.2% PL was found to be attributable to the increased textural properties of kamaboko gels. The shelf-life of kamaboko gels was significantly extended by the addition of 0.2% PL in surimi, especially at 5C and 10C storage.     

ANALYSIS OF SURIMI GEL PROPERTIES BY COMPRESSION AND PENETRATION TESTS

Gel properties of surimi of different quality were analyzed using compression and penetration tests. Parameters used to vary the surimi quality were species, freshness, freeze-abuse and added ingredients. Compressive force at failure was more discriminative than penetration force. The result of a failure response analysis suggests that the compression test is useful in assessing the cohesive property, while the penetration test is better for assessing density and compactness. Good correlations between compression and penetration force values were seen in surimi gels prepared from the same species with and without ingredients, while poor correlations were observed in the surimi which either underwent freeze-abuse or was prepared from different species.     

HEAT-INDUCED GELATION OF MYOSIN IN THE PRESENCE OF ACTIN

ABSTRACT The rabbit muscle contractile proteins, myosin, actin and reconstituted actomyosin were mixed in 0.1–1.0 M KCl, 20 mM buffers, pH 5.0–8.0, and were tested quantitatively for thermally induced gelation properties by measuring the rigidity (shear modulus) of the system at 20–70°. Scanning electronmicroscopy (SEM) was also used to study the structure of the gels formed by gelation of myosin in the presence of F-actin. Under the standard condition, i.e. at 0.6 M KCl, pH 6.0 and 65°, decrease of the myosin/actin mole ratio to about 1.5–2.0 in the reconstituted acto-myosin system resulted in substantial augmentation of the rigidity of the gel formed. Further decreases in the myosin ratio relative to F-actin reduced the rigidity value of the gel to close to the level of myosin alone. Gel-formability of the reconstituted actomyosin was maximal at pH 5.5–6.0 and between 0.5 and 0.8 M KCl and decreased considerably at other pH values and KCl concentrations. The SEM studies revealed progressive changes in three dimensional ordering as actin concentration in the actomyosin varied. These were in concordance with the results of gel strength.     

THERMAL GELATION OF DUCK BREAST AND LEG MUSCLE PROTEINS

Gels were made by heating duck breast and leg myofibrillar protein suspensions (20 mg/ml; pH 5.50, 5.75 and 6.00) at a constant rate of 1C/min from 18C to 70C. After heating the suspensions to 70C at pH 5.50, breast proteins formed gels which were not different (p > 0.05) in strength from leg proteins. At pH 5.75 and 6.00, however, breast proteins formed significantly stronger gels than leg proteins. Increasing the protein suspension pH from 5.50 to 5.75 had no significant effect on the strength of leg protein gels, whereas the strength of breast protein gels more than doubled. A further increase in pH from 5.75 to 6.00 resulted in a three-fold decrease in the strength of leg protein gels; no significant difference was observed for breast gels. Overall, pH 5.75 was suitable for forming strong breast and leg protein gels, whereas pH 5.50 and 6.00 were detrimental for gel formation of breast and leg proteins, respectively. Variations in the gelation behavior of duck breast versus leg protein gelation are characteristic of differences in fiber composition of the muscle types.