A DSC study on the effects of various maltodextrins and sucrose on protein changes in frozen‐stored minced blue whiting muscle

A DSC heat denaturation study on the effects of various maltodextrins and sucrose on protein changes in minced blue whiting muscle during frozen storage at −10 and −20 °C was carried out. All maltodextrins slowed down the decreases in the denaturation enthalpies (ΔH_d) ascribed to myosin and actin, making evident a noticeable effectiveness against protein denaturation, especially at −20 °C. Sucrose was as effective as maltodextrins at −20 °C, but was the least effective treatment at −10 °C. Significant correlations between both ΔH_ds and either protein solubility or formaldehyde production were found at each storage temperature. A low protein sensitivity to the small amounts of formaldehyde produced during the first weeks of storage and errors associated with the determination of enthalpies led to poorer correlations at −20 °C. Maximum denaturation temperatures (T_max) correlated with protein solubility only at −20 °C. No clear relationship between either T_max and the effectiveness of cryostabilisation was found, as T_max also depends on the effectiveness of the treatments against the thermal denaturation of proteins. © 2001 Society of Chemical Industry     

A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) fillets during frozen storage

Changes in the muscle proteins of frozen cod fillets, which produce significant amounts of formaldehyde, and frozen haddock fillets, which produce negligible formaldehyde, were compared. Protein extractability and hydrophobicity and the amino acid contents of soluble and insoluble proteins, as well as formaldehyde formation, were investigated in matching pairs of cod and haddock fillets stored at ?10 and ?30 °C (control). Formaldehyde production in cod was much higher (845 and 1065 nmol g^?1 at 20 and 30 weeks respectively) than in haddock (93 and 101 nmol g^?1 after 20 and 30 weeks respectively) at ?10 °C. However, a rapid decrease in solubility of proteins, increase in hydrophobicity and decrease in the amino acid content of salt‐soluble proteins at ?10 compared with ?30 °C were observed in both species. The results showed that there were no significant differences in the nature of the protein changes between these two species, thus indicating that factors other than formaldehyde were involved in the denaturation of proteins and the formation of aggregates during frozen storage of cod and haddock fillets, especially at ?10 °C. © 2001 Society of Chemical Industry     

Textural Changes and Functional Properties of Cod Mince Proteins as Affected by Kidney Tissue and Cryoprotectants

The addition of cryoprotectants, e.g., a mixture of sucrose and sorbitol or polydextrose (PDT) with sodium hexametaphosphate (SHMP), to improve the texture and water retention properties of cod mince with kidney tissue (modified mince) was studied at ?47°C. Kidney tissue provided trimethylamine oxide (TMAO) demethylase to accelerate dimethylamine (DMA) and formaldehyde formation. Expressible moisture (EM), water uptake ability (WUA), protein solubility, cook loss, DMA production, and textural profile analysis were determined to detect changes in modified mince during frozen storage. Modified mince with SHMP and sucrose/sorbitol or PDT at ?14°C had improved EM, WUA, and cook loss and was more tender.     

Determination of Oxygen Solubility in Liquid Foods Using a Dissolved Oxygen Electrode

A rapid method for determining oxygen solubility in foods was introduced. Fructose, glucose, sucrose, orange juice, apple juice, grape juice, grapefruit juice, lemonade, and tomato juice had similar oxygen solubilities at comparable °Brix readings. The equation: In [ppm O₂] = 2.63 ? 0.0179 (°Brix) ? 0.0190 (°C) estimated to within 5% the oxygen solubility of sugar solutions and fruit juices at temperatures between 4°C and 40°C. At likely food concentrations, citric acid, ascorbic acid, and NaCl reduced oxygen solubility by less than 10%. Tests for component interactions were also conducted. There was no measurable synergism or antagonism between fructose, glucose, and sucrose with or without organic acids.     

Development of a spray-dried conjugated whey protein hydrolysate powder with entrapped probiotics

Bifidobacterium animalis ssp. lactis ATCC27536 and Lactobacillus acidophilus ATCC4356 were encapsulated in a conjugated whey protein hydrolysate (WPH10) through spray drying. Probiotic cultures were added at the ratio of 1:1 into the conjugated WPH10 solution at a spiking level of about 10 log₁₀ cfu/mL. The mixture was spray dried in a Niro drier with inlet and outlet temperatures of 200°C and 90°C, respectively. The final dried product was determined for cell viability and further stored for 16 wk at 25°, 4°, and ?18°C to monitor viability and functionality. Micro images showed the presence of link bridges in non-conjugated WPH10, whereas, in the case of conjugated WPH10, round particles with pores were observed. The mean probiotic counts before and after spray drying were 10.59 log₁₀ cfu/mL and 8.98 log₁₀ cfu/g, respectively, indicating good retention of viability after spray drying. The solubility and wetting time of the WPH10-maltodextrin (MD) encapsulated probiotic powder were 91.03% and 47 min, whereas for WPH10, the solubility and wetting time were 82.03% and 53 min, respectively. At the end of storage period, the counts were 7.18 log₁₀ cfu/g at 4°C and 7.87 log₁₀ cfu/g at ?18°C, whereas at 25°C the counts were significantly reduced, to 3.97 log₁₀ cfu/g. The solubility of WPH-MD powder was 82.36%, 83.1%, and 81.19% at ?18°C, 4°C, and 25°C, respectively, and wetting times were 61 min, 60 min, and 63 min at ?18°C, 4°C, and 25°C, respectively. By contrast, for WPH10 powder, the solubility significantly reduced to 69.41%, 69.97%, and 68.99% at ?18°C, 4°C, and 25°C, and wetting times increased to 71 min, 70 min, and 72 min at ?18°C, 4°C, and 25°C, respectively. The conjugated WPH10 is thus demonstrated as a promising carrier for probiotics and can be further used as an ingredient for developing functional foods, to harness their enhanced functionality and health benefits derived from both WPH and probiotics.     

Protein denaturation in frozen fish]

To inhibit the rapid deterioration of the production-technological properties of fish meat minced and frozen on board, it is necessary to become acquainted with the causes of protein denaturation under these conditions. It was found that the protein solubility in codfish is impaired by formaldehyde which develops from trimethyl-amine oxide during storage and also by the salt content. After 7 days at -20 degrees C, the solubility of the sarcoplasmic and myofibrillary proteins in minced fish meat added with 80 mg of formaldehyde per 100 g of total protein amounted to almost 70% and 35%, respectively, of the value determined in controls, i.e., samples without formaldehyde. After this period of storage, only 30% of the added formaldehyde were in the free state. After 1 month, the solubility of the myofibrillary proteins in waterleached fish meat was by 30% higher than in unleached controls, 80 mg of formaldehyde per 100 mg of total protein having been added in both cases. After 1 month at -5 degrees C and -20 degrees C, only 90 and 15 p.p.m. of formaldehyde, respectively, were found in minced fish meat, whereas leached samples contained no formaldehyde. The solubility of the myofibrillary proteins in leached fish meat (the initial salt content of which had been restituted) was by 30% lower than in the unleached controls.     

Localization of formaldehyde production during frozen storage of European hake (Merluccius merluccius)

The formation of dimethylamine and formaldehyde from trimethylamine N-oxide by the enzyme trimethylamine N-oxide demethylase in whole hake during frozen storage was studied. The objective was to check if there were parts of the muscle with a higher production of dimethylamine and formaldehyde, and if the presence of kidney during frozen storage had any significant influence on the production. Three variables were examined through one year storage. The first was anatomical location, considering the red muscle and three zones of white muscle, one located right over the kidneys, the dorsal part over the viscera, and the tail. The second variable was the temperature of storage, -11 °C or -18 °C. Finally, the influence of kidneys during storage, comparing fish with and without kidneys, was also evaluated. No differences were found in dimethylamine and formaldehyde production between fish with and without kidneys stored at -18 °C. However at -11 °C the amounts of dimethylamine and formaldehyde detected in fish without kidneys were, in some cases, higher than in those with kidneys. Kidney removal does not have a statistically significant influence on DMA and FA production in frozen storage hake. Differences in dimethylamine and formaldehyde values among different anatomical locations were found, especially in those stored over one year. It was found that, in general, the white muscle located right over the kidneys produced more dimethylamine than other parts of the fish.     

Effect of dry heat stabilisation on the functional properties of rice bran proteins

Rice bran was stabilised by dry heat method at 120 °C for 10–60 min, and then, protein was extracted from stabilised rice bran using weak alkali method. The storage characteristics of stabilised rice bran and the influences of dry heat pretreatment on the physicochemical properties of rice bran protein isolate were also evaluated. The results indicated that dry heat pretreatment could not only prevent rancidity of rice bran effectively, but also improve some functional properties of rice bran proteins, such as emulsifying properties, oil holding capacity, and water holding capacity. However, foaming properties and protein solubility were slightly destroyed because of heating. Rice bran was pretreated at 120 °C for 10 or 20 min and then extracted at pH 9.5, and the protein yields were 50.09% and 46.98%, respectively. Therefore, the dry heat treatment at 120 °C for 10 or 20 min was a suitable alternative process in stabilisation of rice bran.     

Maltoheptaose and maltooctaose as the superior aroma encapsulating agents

Maltoheptaose (G7) and maltooctaose (G8) were examined as potential encapsulating agents for aroma compounds and compared with commercially available maltodextrins with the dextrose equivalent (DE) 10 and 18. Solutions of each encapsulating agent were homogenized with aromas and spray dried. The initial amounts of aroma compounds retained in each encapsulating agent were as follows: G7<G8≈DE 18<DE 10. During storage at 25°C, G8 was most effective at retaining the aroma compounds among 4 encapsulating agents used in this study, then followed by G7. This result may be due to the high molecular weight and uniform wall matrix composed of either pure G8 or G7 when compared to the commercial maltodextrins that had a broad distribution of molecular weights. Our results suggest that G7 and G8 can serve as excellent encapsulating agents for aroma compounds.     

Diffusion of Sucrose in Osmo-Dehydrofrozen Apple

Apple parallelepipeds were dewatered by osmosis in sucrose solution at 30°C for 3 h, and at 70°C for 1 h. Dewatered material was air-frozen at ?12, ?20, and ?35°C and stored for 1, 3, and 6 months. After a prescribed time of storage, cryoscopic temperature, amount of non-frozen water, and effective diffusion coefficients were calculated based on sucrose concentration profiles in the frozen material. In frozen, osmotically dewatered apple, mass transfer was very slow. After 6 months of storage, large concentration gradients still occurred in the frozen material. Effective diffusion coefficients, based on sucrose concentration expressed as percent of the total mass of the sample, were statistically not dependent on storage temperature. They were dependent on sucrose concentration and varied from 2·10^?14 m²/s, at high sucrose concentration, to 5·10^?11 m²/s, at low sucrose concentration. On the other hand, effective diffusion coefficients, based on the sucrose concentration in non-frozen water, were dependent on storage temperature and sucrose concentration as well. They were from 1·10^?15 m²/s to 2·10^?12 m²/s.     

Production and Size Distribution of Rice Maitodextrins Hydrolyzed from Milled Rice Flour using Heat-Stable Alpha-Amylase

Maltodextrins were produced from milled rice flour in a single-step process using a heat-stable α-amylase preparation. The starting solids content was 30% (w/w), and processing temperatures and times were varied between 70–97°C and 15–75 min, respectively. Optimum liquefied starch yields, which accounted for virtually all of the starch present, were obtained at temperatures of 80°C and above, but reducing sugars and DE values were highest at 70°C. Low molecular weight saccharide concentrations (DP 1–10) were greatest at 80°C. Because processing at temperatures of 90–97°C resulted in decreased levels of reducing sugars and DP 1–10 concentrations without providing a substantial increase in solubilized starch yields, it was concluded that rice maltodextrins could be most effectively produced at a processing temperature of 80°C.     

In Vitro and Mouse Evaluation of Methods for Protecting Whey Protein and Casein from Ruminal Degradation

A series of in vitro buffer (protein solubility) and rumen fermentation (ammonia production) studies were conducted to evaluate varying formaldehyde (.25, .5, 1, and 3%) and tannic acid (.5, 1, 2, 3, and 6%), and three heating times (1, 2, and 3 h at 104 C) on protection of whey protein concentrate and casein from ruminal degradation. Subsequent trials of mouse growth were conducted to evaluate the effectiveness of protection of treated proteins. Formaldehyde (.25 to 3%) reduced solubility of whey protein and casein to less than 10% of the untreated in pH 6.8 buffer and approximately 30% of the untreated in pH 2.5 buffer plus pepsin. Formaldehyde reduced ammonia production, indicating protection and reduced solubility of whey protein and casein under rumen conditions in vitro. Tannic acid (.5 to 6%) did not greatly reduce protein solubility and ammonia production. Heat treatment reduced protein solubility to less than 10% of the untreated in pH 6.8 buffer and to 50% of the untreated in pH 2.5 buffer and reduced ammonia production to approximately 20% of the untreated. Growth and feed intake of mice were decreased with 1% formaldehyde treated diets (17% protein), indicating overprotection of protein. Growth decreased as tannic acid increased. Mouse growth also decreased as the length of heat treatment increased. Diets with .5% formaldehydecasein depressed gains. Based on these in vitro and mouse-evaluation studies, formaldehyde less than .5% of the dry weight is required to protect whey protein and casein from ruminal degradation and permit solubilization in the lower intestinal tract.     

Quality changes during the storage of apple puree

The stability of apple puree at different constant temperatures (-18°C, 4°C, 20°C, 50°C and 60°C) was studied within the period of 30 days. During this time changes in the samples of apple puree, which was stored at variable temperature, were determined as well. The content of ascorbic acid, the sucrose inversion, the formation of furfural and levulinic acid as well as sensory properties were followed as criteria of the puree quality. From obtained data the temperature dependence of these reactions was derived. On this base the shelf life of apple puree (the time, after which the sensory differences became significant) was estimated. This period was relatively short, i.e. less than 100 days at 20°C. The changes in puree at variable temperature were similar to those at higher storage temperatures (40°C–50°C).     

Optimisation of processing variables affecting the osmotic dehydration of pomegranate arils

For the optimisation of osmotic dehydration by response surface methodology, the experiments were conducted according to Central Composite Rotatable Design (CCRD) with three variables at five levels. The low and high levels of the variables were 40 and 50 °C for osmotic solution temperature, 45 and 55°Bx for sucrose solution concentration, 60 and 100 min for duration of dipping in osmotic solution, respectively. The fruit to solution ratio was kept 1:4 (w/w) during all the experiments. Before dipping the arils in sucrose solution, the freezing of the whole pomegranate at ?18 °C was carried out to increase the permeability of the outer cellular layer of the arils. The arils were further convectively dehydrated at 60 °C air temperature up to final moisture content of 10% (wb) to make it a shelf stable product. The optimum conditions for osmotic solution concentration, temperature and process duration were 55°Bx, 40 °C and 100 min, respectively.     

Studies on fish muscle protein. Nutritional consequences of the changes occurring during frozen storage

Samples of cod, whiting, herring, lemon sole and skate muscle were frozen and stored at ? 8°C for up to 20 months. Samples of cod muscle were also stored at ? 30°C. During storage at ?8°C the decrease in the solubility of the muscle proteins in 5% NaCl (denaturation) was most rapid in whiting followed in order by skate, cod, herring and lemon sole. Little change was detected in the NaCl solubility of cod muscle protein stored at ? 30°C. An increase in the pH was found to occur in all the species examined. The relationship between these changes and the toughening that occurs in fish muscle during frozen storage is considered. No nutritionally significant decrease in the lysine availability or the in vitro digestibility of the muscle proteins was found to occur in any of the species examined. In whiting, lemon sole and skate very small, statistically significant, increases in the available lysine content were detected after 7 months of storage at ?8°C and this may indicate that unfolding of the protein chains had occurred.     

Structural and thermodynamic features of covalent conjugates of sodium caseinate with maltodextrins underlying their functionality

The sodium caseinate (SCN)-maltodextrin (MD) covalent conjugates were prepared by a food-grade process involving the first step of the Maillard reaction. The covalent conjugates were prepared with different weight ratios of biopolymers (R(MD?:?SCN) = 0.4; 1; 2; 5) in the system using maltodextrins of strongly different dextrose equivalents (DE), i.e., DE = 2 and 10. We have observed that the covalent conjugation of SCN with MD, in contrast to their simple mixing, improved the protein solubility in an aqueous medium in a wide pH range that was more pronounced in the vicinity of the SCN isoelectric point (pH 3.8-4.4). The extent of SCN solubility was mainly governed by the weight/molar ratio of the biopolymers in the covalent conjugates, R(MD?:?SCN). Data of static multiangle laser light scattering showed that the revealed increase in the solubility of the conjugates could be predominantly attributable to the dramatic increase in their thermodynamic affinity for an aqueous medium. Which was most pronounced for the maltodextrin with the higher DE (DE = 10). The direct relationship between the increase in the solubility of the conjugates and the increase in their foaming ability, as compared against SCN, has been revealed as a rule both at neutral pH and at the pI. In addition, the found improvement in the protein foaming ability was also defined by both the weight/molar ratio (R(MD?:?SCN)) and the dextrose equivalent of the maltodextrins attached to the protein.     

Chemical Stability of Antioxidant-Washed Beef Heart Surimi During Frozen Storage

Beef heart surimi was prepared in the presence or absence of propyl gallate and blended with or without cryoprotectants (sucrose, sorbitol). Samples were stored at -15, -29, and -70°C for 0.2, 2, 4, 12, 26 and 52 wk to observe oxidative changes in lipids (TBARS and dienes) and proteins (sulfhydryl, carbonyl, surface hydrophobicity, and myosin ATP-ase). Lipid and protein oxidation was minimal at -70°C. The freeze-thaw process caused lipid and protein oxidation in control samples at -15 and -29°C. Oxidation increased rapidly after 4 wk. Propyl gallate inhibited lipid oxidation but was ineffective against protein changes. After 12 wk, cryoprotectants promoted lipid and protein oxidation in the absence of propyl gallate.     

Heterogeneous base catalytic transesterification synthesis of sucrose ester and parallel reaction control

The equilibrium solubility of sucrose in methyl stearate, methyl oleate and methyl laurate with or without the addition of surfactants was investigated. The side reactions, pyrolysis of the sucrose, glucose and fructose, are also discussed through studying their data of differential thermal analysis and thermal gravimetric analysis. Results show that the solubilities of sucrose in methyl esters of fatty acids range from 0.01 g/100 g to 0.21 g/100 g in a surfactant‐free system with the temperature range of 40–140 °C. The addition of surfactants increased the sucrose solubility in the fatty acid esters. Under the strict anhydrous conditions, the soap concentration can be controlled at a very low level. With the increase in the temperature, sucrose began to decrease in weight at 225 ± 5 °C, glucose began to decrease in weight at 85 ± 5 °C, and fructose began to decrease in weight at 170 ± 5 °C.     

Highly Concentrated Branched Oligosaccharides as Cryoprotectant for Surimi

Freeze-thawing studies at different concentrations, using an actomyosin solution (extracted from Alaska pollock), revealed that an 8% (w/v) solution of oligosaccharides mixture (HBOS) was most effective in cryoprotection. During frozen storage (-18°C), HBOS showed cryoprotective effects similar to sucrose and a sucrose+sorbitol mixture (1:1). Surimi gel prepared with HBOS showed higher hardness and more dense microstructure than others, although water holding capacity was slightly lower than the gel with sucrose+sorbitol. HBOS containing gel showed lower whiteness than sucrose but no difference with sucrose+sorbitol. HBOS appeared to have good potential as a non-sweet cryoprotectant of fish protein.     

Banana Shrimp, Penaeus merguiensis, Quality Changes During Iced and Frozen Storage

Shelf life of banana shrimps, Penaeus merguiensis, were studied along with formaldehyde changes in their muscles during iced and frozen storage. K-value, timethylamine oxide nitrogen (TMAO-N), trimethylamine nitrogen (TMA-N), volatile basic nitrogen (VB-N) and sensory quality were determined. Shelf life was 4 days in ice, 6 days at -3°C and 9 wk at ??10°C. They remained acceptable after 6 mo at ?20°C. Formaldehyde was a good indicator in shrimp shelf life assessment.