Physicochemical and textural properties of dried squid as affected by alkaline treatments

The effect of alkaline treatment on the physicochemical and textural properties of dried squid was investigated. Dried squid soaked in 0.15 mol kg⁻¹ sodium carbonate with a squid/alkaline solution ratio of 1:10 (w/v) for 20 h was shown to be the most acceptable in terms of both appearance and textural properties. Sodium hydroxide appeared to extensively destroy the fibre structure, leading to a mushy texture of dried squid. Alkaline‐treated squid had increased moisture and ash contents but decreased shear force compared to dried squid. Alkaline treatment effectively disrupted various bonds stabilising the fibre structure, resulting in structural alteration and increased water absorption. Scanning electron microscopy (SEM) showed that alkaline treatment mainly contributed to swelling and disintegration of squid muscle fibre. As a result, dried squid acquired a softened texture with a higher water‐holding capacity. © 2000 Society of Chemical Industry     

Rheological Properties of Dried Squid Mantle Change on Softening

TO CLARIFY differences between raw squid and softened dried squid, dried squid mantle was softened under various conditions, degree of swelling and certain properties were measured, and the musculature was examined by electron microscopy. Swelling the dried squid to the original level of raw squid required softening in three steps: presoaking, alkali-soaking, and post-soaking. The alkali-soaking was mainly responsible for the swelling effect. Resulting properties were largely changed from those of raw squid. Electron microscopy showed much water permeation throughout the muscle fibrils and fibers, while there was almost no permeation of water inside the individual fibrils.     

Lysyl oxidase from jumbo squid (Dosidicus gigas) muscle: purification and partial characterization

Lysyl oxidase (LOX; E.C.1.4.3.13) was purified from jumbo squid muscle (Dosidicus gigas) with 1900‐fold and yield 1.9%, and characterized for the first time. The purification procedure consisted of fractionation with urea and a combination of size‐exclusion and anion‐exchange chromatography. The enzyme had a molecular weight of 32 kDa, as estimated by SDS‐PAGE. Using a specific LOX substrate (1,5‐diaminopentane), its optimum activity was determined at pH 8.2 and 65 °C. Activation energy (E_a) of the enzyme was 69.94 kJ K^?1 mol^?1. The enzyme was strongly inhibited by β‐aminopropionitrile fumarate (BAPN), a specific LOX inhibitor. Moreover, purified LOX was able to work at different temperatures (20–90 °C) at pH 8.2. Although further research is needed, the results from this work suggest that based on LOX activity, this enzyme may be of practical use in preventing textural changes in jumbo squid during storage or processing.     

Synergistic mechanism of steam blanching and freezing conditions on the texture of frozen yellow peaches based on macroscopic and microscopic properties

Freezing and blanching are essential processing steps in the production of frozen yellow peaches, inevitably leading to texture softening of the fruit. In this study, the synergistic mechanism of stem blanching, freezing conditions (−20°C, −40°C, −80°C, and liquid nitrogen [−173°C]), and sample sizes (cubes, slices, and half peaches) on macroscopic properties of texture, cellular structure, and ice crystal size distribution of frozen yellow peaches were measured. Blanching enhanced the heat and mass transfer rates in the subsequent freezing process. For nonblanched samples, cell membrane integrity was lost at any freezing rate, causing a significant reduction in textural quality. Slow freezing further exacerbated the texture softening, while the ultra-rapid freezing caused structural rupture. For blanched samples, the half peaches softened the most. The water holding capacity and fracture stress were not significantly affected by changes in freezing rate, although the ice crystal size distribution was more susceptible to the freezing rate. Peach cubes that had undergone blanching and rapid freezing (−80°C) experienced 4% less drip loss than nonblanched samples. However, blanching softened yellow peaches more than any freezing conditions. The implementation of uniform and shorter duration blanching, along with rapid freezing, has been proven to be more effective in preserving the texture of frozen yellow peaches. Optimization of the blanching process may be more important than increasing the freezing rate to improve the textural quality of frozen yellow peaches.     

Biochemical and nutritional changes in fish proteins during drying

Biochemical and nutritional changes in the muscle proteins of a lean marine fish Nempiterus japonicus during drying at 50, 60 and 70°C were investigated. Solubility of proteins in water, 0.6 M NaCl, 1.5 M urea, 8 M urea and 10 g litre^?1 sodium dodecyl sulphate (SDS) decreased as drying progressed at all three temperatures; most of the decrease occurring in the initial 4 h of drying SDS-polyacrylamide gel electrophoresis of 1.5 M urea, 8 M urea and SDS extracts showed that higher molecular weight (MW) protein fractions were more sensitive to drying and disappeared much earlier from electropherograms than the lower MW protein fractions. Residual solubility of proteins near the pH range of 4–6 was found to increase during drying, but solubility at acid and alkaline pH was adversely affected. Decrease of solubility by drying was more affected at acid pH, especially at higher temperatures than at alkaline pH. Sulphydryl groups registered a regular and sharp decrease with drying except at 50°C, where initially an increase was observed. Apart from disulphide and hydrophobic bonds, free amino groups also appear to be involved in denaturation reactions during drying. Pepsin digestibility of fish muscle decreased slightly during drying but a clear relationship with drying temperature was not evident. Highly significant differences in proteins between protein efficiency ratio (PER), net protein utilisation (NPU) and biological value were observed between the drying temperatures. The PER and NPU of fish dried at 60°C were significantly higher than those dried at 50 or 70°C.     

Functional modification of vital wheat gluten with corn syrup using hydrothermal treatment

Functional properties of gluten modified using hydrothermal treatment were compared with those of vital wheat gluten (VWG). Gluten slurry was jet cooked under pressure in the presence of corn syrup (CS) at different temperatures (121 and 149 °C) for different times and then spray dried. Foaming properties for all samples (treated and untreated) at different pHs showed that, although the optimum pH was 5, at this pH the treated gluten samples displayed reduced foaming properties as compared with the control, whereas at all other pHs there was an increase in foaming properties. The sample treated with CS at 121 °C (JC121w/cs) showed the highest viscosity and elasticity increase among all treated samples. Emulsifying properties were adversely affected by an increase in temperature of treatment, whilst addition of CS helped to restore emulsion stability (ES). The sample VWG with CS (Cont.w/cs) at pH 3 showed maximum ES. In general, samples after treatment showed increased solubility. The hydrophilic but non‐ionisable sugar hydroxyl groups affected the functionality at lower pH. Molecular changes were followed by size exclusion high‐performance liquid chromatography (SE‐HPLC) and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE). Samples subjected to the lower temperature (121 °C) showed a shift of the molecular weight distribution to higher values in the HPLC profile, consistent with higher viscosities for this treatment. For the same samples, SDS‐PAGE of the reduced protein exhibited a decrease in the intensity of bands corresponding to high‐molecular‐weight glutenin subunits, complementing the fact that large‐molecular‐size polymers are involved during protein modification. Copyright © 2005 Society of Chemical Industry     

AMINO ACID COMPOSITION AND IN VITRO PROTEIN DIGESTIBILITY OF DRIED SQUID REHYDRATED IN WATER AND ALKALI

Crude protein content, amino acid composition and in vitro protein digestibility of fresh, dried and rehydrated Argentina squid (Illex argentinus) were studied. Most of the nonamino acid nitrogenous compounds in the mantle muscle dissolved in water during rehydration. Rehydration improved the nutritive value of protein in dried squid. Rehydration decreased the concentration of proline relative to total amino acids in muscle. Aromatic amino acids were limiting essential amino acids in fresh and dried squid but not in rehydrated squid. Amino acid scores increased with the extent of rehydration, more so in alkali than in water. The alkali rehydration also increased the in vitro protein digestibility of dried squid.     

Effect of Freezing and Microwave Heating on Proteins from Codfish Fillets: Analysis by SDS Polyacrylamide Gel Electrophoresis

Water soluble and insoluble proteins were extracted from codfish samples subjected to a rapid freeze (– 196°C), a slow freeze (– 15°C), 1 min microwave heating, and from fresh extracts. The water soluble protein content decreased significantly in both frozen samples and in the microwave heated samples when compared to fresh extracts. Analysis by SDS PAGE showed a significant loss in water soluble proteins after microwave treatment concomittant with the appearance of two high molecular weight species. No differences were apparent in the nonsoluble protein SDS PAGE profiles.     

Lysyl oxidase from jumbo squid (Dosidicus gigas) muscle: detection and partial purification

Lysyl oxidase (LOX) was detected and partially purified from jumbo squid (Dosidicus gigas) muscle, for the first time. A procedure for the purification of LOX from jumbo squid muscle which consisted of urea extraction, Sephadex G‐75 and anion exchange chromatography was developed. Activity of partially purified LOX was 390‐fold higher than the original extract. Two protein fractions with 32 and 24 kDa were detected by SDS‐PAGE. The enzyme was strongly inhibited by β‐aminopropionitrile fumarate, a specific LOX inhibitor. LOX was purified with 3.8% yield, showing a specific activity of 0.078 IU mg^?1 protein. This knowledge will help understand the behaviour of jumbo squid protein during cool storage or manufacture.     

Polyphenol Oxidase from Apple (Malus domestica Borkh. cv Bramley's Seedling): Purification Strategies and Characterization

ABSTRACT Polyphenol oxidase (PPO) was isolated from Bramley's Seedling apples with 75.7‐fold purification and 26.5% recovery by ammonium sulfate precipitation, phenyl sepharose chromatography, ion exchange chromatography, and hydroxyapatite chromatography. Molecular weight was estimated to be about 45 kDa by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS PAGE). Optimum PPO activity was at pH 6.5 and greater than 50% activity was retained during storage for 72 h at pH 5.5 to 6.5. Optimum temperature for activity was 30 °C and the enzyme had residual activity of greater than 50% during storage for 72 h at 20 °C to 30 °C and for 24 h at 40 °C to 50 °C. Of the substrates tested, activity was greatest with 4‐methylcatechol followed by catechol, pyrogallol, and (?)epicatechin. The most effective inhibitors tested were sodium metabisulfite and ascorbic acid.     

Muscle Firmness and Structure of Raw and Cooked Arrow Squid Mantle as Affected by Freshness

Changes in firmness and structure of arrow squid (Loligo bleekert) mantle muscle during refrigeration (5°C) were studied. Shear force of raw mantle decreased sharply between 3 and 9 h refrigeration after killing. Light microscopic observations showed many pores between muscle cells in the softened raw samples. Transmission electron microscopic observations suggested that the spaces appeared as a result of detachment of muscle cells from connective tissues. After cooking the stored raw muscle, the shear force and muscle structure were almost the same for samples with different storage times. Freshness had an influence on raw squid muscle firmness and structure but not on cooked muscle.     

Texture of Cooked Mantle of Squid lllexargentinus as Influenced by Specimen Characteristics and Treatments

Boiling frozen stored squid in 2% NaCl solution caused 30% weight loss after 5 min but changes in protein solubility and softening of the meat continued for at least 45 min. The influence of variability within the species on the texture of the cooked product was more significant than that of frozen storage. In discolored squid significant proteolysis was shown by electrophoresis. Such meat was less tough than that from nondiscolored specimens. Acetic acid cure induced proteolysis without improving texture, while polyphosphates softened the product without detectable proteolysis. The decisive effect on texture was displayed by pH and polyphosphates. Heating at 80° and 90°C left an uncooked sensory note.     

Isolation,purification and characterisation of polygalacturonase from ripened banana (Musa acuminata cv. Kadali)

Bananas are the most important fruit crop in the world. Short shelf life of the fruit is the major limiting factor in international trade, and this is due to the softening of the pulp during ripening. Fruit softening is an important aspect of ripening process in fleshy fruits and is caused by the cumulative action of a group of cell wall‐modifying enzymes. Polygalacturonase (PG) is the key enzyme involved in the fruit softening process in banana, and this study reports the isolation, purification and characterisation of polygalacturonase enzyme from ripened fruits of a delayed ripened banana cultivar found specifically in Kerala (Musa acuminata cv. Kadali). PG was purified by ammonium sulphate fractionation followed by DEAE cellulose ion exchange chromatography and gel filtration using Sephadex G 100. The purified protein showed two subunits on SDS‐PAGE and a single band on native PAGE. Enzyme showed maximum activity at pH 3.5 and 40 °C. Fe³⁺ enhanced the activity more, while Mg²⁺ and Ca²⁺ slightly stimulated the activity of purified enzyme. Km value for substrate polygalacturonic acid was 0.06%.     

Effect of extrusion cooking on structure and functional properties of pea and kidney bean proteins

Pea (Pisum sativum L cv Ballet) and kidney bean (Phaseolus vulgaris L cv Pinto) seeds were extruded at 148 and 156 °C respectively. Protein solubility at various pH values and in various solvents was determined and analysis of protein fractions was carried out by SDS‐PAGE. Also, sulphhydryl and disulphide groups, water‐holding capacity (WHC), water solubility index (WSI) and oil absorption capacity (OAC) were determined. No changes in total nitrogen content of pea and kidney bean seeds occurred as a result of thermal treatment. Protein solubility from raw and extruded legumes was significantly higher in saline solutions than in water in the pH range 2–10. The solubility of proteins from extruded pea and kidney bean flours was greatly decreased with respect to native flours when extraction was in buffer (pH 7.0) alone. Extraction with buffer containing 2‐mercaptoethanol (2‐ME) or sodium dodecyl sulphate (SDS), alone or in combination, greatly increased protein extractability. As a result, the relative solubility was nearly 100% in buffer with SDS and 2‐ME for both raw and extruded samples. Total and free sulphhydryl group and disulphide contents decreased significantly (P < 0.05) after extrusion cooking. Moreover, extrusion treatment caused major changes in the band patterns of the albumin and globulin fractions obtained by SDS‐PAGE. WHC and WSI of extrudates increased significantly in both peas and kidney beans. A significant reduction in OAC was observed in extruded kidney bean flour. © 2000 Society of Chemical Industry     

Improvement in emulsifying properties of soy protein isolate by conjugation with maltodextrin using high‐temperature,short‐time dry‐heating Maillard reaction

Soy protein isolate (SPI)–maltodextrin (MD) conjugates were synthesised using Maillard reaction under high‐temperature (90, 115 and 140 °C), short‐time (2 h) dry‐heating conditions. The loss of free amino groups in proteins and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE) profile confirmed that SPI‐MD conjugates were formed and higher dry‐heated temperatures could increase the glycosylation degree. The emulsifying properties of SPI and SPI‐MD conjugates were evaluated in oil‐in‐water emulsions. The emulsions stabilised with SPI‐MD conjugates synthesised at 140 °C exhibited higher emulsifying stability and excellent storage stability against pH, ionic strength and thermal treatment compared with those synthesised at 90 °C, 115 °C and SPI stabilised emulsions. This might be due to a greater proportion of conjugated MD in SPI‐MD conjugates synthesised at 140 °C because of the higher glycosylation degree, and more conjugated MD on the droplet surface could provide steric effect and enhance the stability of the droplets in the emulsions.     

Postmortem Changes in Mule Duck Muscle Marinated in Red Wine

Postmortem changes in duck breast muscle as affected by red wine marination at 5 °C were studied. Myofibrils were purified from the control (CON) and the red wine marinated muscle (RW) after 0, 1, 3, 7, and 14 d storage. The results showed that myofibril fragmentation index (MFI) was significantly (p < 0.05) higher in RW than in CON samples. Myosin heavy chain, α‐actinin, troponin‐T, titin, and nebulin were degraded more rapidly as seen on SDS‐PAGE in RW than in CON samples. Our results suggested that red wine marination can cause postmortem changes in mule duck breast muscle.     

Thermal Gel Degradation (Modori) in Sturgeon (Acipenseridae) Surimi Gels

Sturgeon meat has been found to be suitable as surimi raw materials. The present study determined the modori phenomenon in sturgeon surimi gels and identified its relationship with cathepsins. In all heat‐treated gels (25 to 90 °C, at 5 °C intervals), the 40 °C‐incubated sturgeon surimi gel showed the weakest gel properties and water‐holding capacity (P < 0.05), a rough protein gel network under SEM, and the highest protein solubility and trichloroacetic acid‐soluble peptides content (P < 0.05). SDS‐PAGE indicated that the myosin heavy chain band of sturgeon surimi gels was almost completely degraded at 40 °C. Moreover, the highest cathepsin L activity was observed in 40 °C‐treated sturgeon surimi gels (P < 0.05). Our results suggested that the modori phenomenon in sturgeon surimi gels occurred at 40 °C, which was partially attributed to cathepsin L, thereby allowing for the better exploitation and utilization of sturgeon surimi.     

Study on the self‐assembly property of type I collagen prepared from tilapia (Oreochromis niloticus) skin by different extraction methods

Type I collagen was prepared from tilapia (Oreochromis niloticus) skin by acetic acid and pepsin process at 4 °C, respectively (ASC and PSC), and hot‐water method separately at 25, 35 and 45 °C (C‐25, C‐35 and C‐45). Their structure and self‐assembly property were discussed. SDS‐PAGE patterns suggested that pepsin hydrolysis and the 35 and 45 °C extraction produced collagen with much reduced proportions of α‐ and β‐chains. Fourier transform infrared spectroscopy spectra revealed that pepsin hydrolysis did not change the conformation of collagen, but higher extraction temperature did. Self‐assembly curves and atomic force microscopy (AFM) observations showed that only ASC, PSC and C‐25 could self‐assemble into fibrils with D‐periodicity, but the reconstruction rate of C‐25 was lower. Besides, PSC had relatively higher resolution ratio compared with others. Overall, pepsin‐extracted collagen displayed higher solubility and better fibril‐forming capacity, having the potential of applying in biomaterials and food‐packaging materials.     

The impact of collagen on softening of grass carp (Ctenopharyngodon idella) fillets stored under superchilled and ice storage

The objective of this work was to study the impact of collagen on softening of grass carp (Ctenopharyngodon idella) fillets during chilled storage. The fillets were stored under superchilling (?1.5 ± 0.2 °C) and with ice (0.2 ± 0.1 °C) for 21 days, and texture properties, collagen and the related enzyme activities were measured. Results showed that firmness and collagen content were strongly influenced by storage temperature and time. Fillet firmness decreased by 32.3% (superchilling) and 49.6% (ice stored) of the initial values after 3 days of storage, respectively. Total collagen content decreased with time, but different collagen fractions showed variations. Collagen degraded to different extents depending on storage conditions as indicated by SDS‐PAGE and amino acid analysis. In addition, collagenase activity declined significantly during the first 3 days, followed by a slow increase. This study demonstrated that collagen degradation was involved in grass carp fillet softening and provided useful information for fillet quality improvement.     

INFLUENCE OF HARVEST SEASON ON THE PROTEOLYTIC ACTIVITY OF HEPATOPANCREAS AND MANTLE TISSUES FROM JUMBO SQUID (DOSWICUS GIGAS)

Jumbo squid (Dosidicus gigas) size and protease activities were evaluated after harvest in April (A) and November (N). A were smaller (560±120 g vs 6040±1130 g) and hepatopancreas was a larger percent of body weight (8.3±2.5 vs 4.6±2.1). Mantle from A had lower water (73.9±l.l vs 79.1± 1.2) and higher protein (29.0±1.1 vs 23.1±0.8). Lipid and protein contents of N and A hepatopancreas tissues did not differ (P < 0.05). Azocaseinolytic, trypsin‐like, chymotrypsin‐like, aminopeptidase, and carboxypeptidase activities were detected in mantle (ME) and hepatopancreas extracts (HPE). HPE and ME from N had higher activity than A for all substrates (P < 0.05). With azocasein substrate, HPE activity from A had a pH optimum of 5 ‐ 6 and a temperature optimum of 70C, whereas HPE from Nhad highest activity at pH 9 and 40–70C. ME from A had maximum proteolytic activity at pH 6 and 60C, whereas that from N had maximum activity at pH 10 and 40C. SDS‐PAGE zymograms of HPE from A and N revealed different patterns of activity and 1 and 2 major protease zones, respectively.