The amino acid composition,solubility and emulsifying properties of sweet potato protein

A protein was purified from the high-protein type sweet potato variety 55-2 available in China. The amino acid composition, solubility and emulsifying properties of the sweet potato protein (SPP) were studied. The SPP was rich in aspartic acid (18.5%) and glutamic acid (9.30%) while essential acid amino acids made up approximately 40.7% of the SPP. The SPP was highly soluble in distilled water over a wide range of pH. However, solubility of the SPP in 1.0 M NaCl and 1.0 M CaCl₂ solutions was low especially at pH below the pI of the SPP. The SPP in CaCl₂ demonstrated emulsifying activity index (EAI) and emulsion stability index (ESI) many folds higher than those in distilled water and NaCl solution (P < 0.05).     

Peeling,drying temperatures,and sulphite-treatment affect physicochemical properties and nutritional quality of sweet potato flour

The effects of peeling, drying temperature (55–65 °C) and pretreatment on the physicochemical properties and nutritional quality of sweet potato flour were investigated. The flours were prepared from peeled and unpeeled sweet potatoes dipped in 0.5% sodium hydrogen sulphite (NaHSO₃). There were significant differences (p < 0.05) in ΔE values and browning index between flours from peeled and unpeeled sweet potatoes without sulphite-treatment (PF and UF). On the other hand, flours from peeled and unpeeled sweet potatoes with sulphite-treatment (PSF and USF) had higher L∗, a∗, and b∗ values, swelling capacity, ascorbic acid, and total phenolics than PF and UF. However, USF and UF had higher β-carotene content than PSF and PF. β-Carotene and ascorbic acid contents decreased with increasing drying temperature for all flours, whereas total phenolics increased for PSF and USF. Therefore, the best quality product was obtained when samples were pretreated with sulphite before drying at any temperature.     

Effects of temperature and pH on the kinetics of caramelisation,protein cross-linking and Maillard reactions in aqueous model systems

Solutions of either glucose, bovine serum albumin (BSA), casein, glucose–BSA or glucose–casein were heated at 60 to 100 °C at pH 8.0 and pH 9.7, and the kinetics of the reaction markers (disappearance of the glucose and amino groups, development of UV absorbance and browning, and protein reticulation) were monitored. All the markers were enhanced at increasing temperatures, and, except for the disappearance of the free amino group and protein polymerisation, at alkaline pH levels. The loss of the amino group occurred in parallel with increase in polymerisation. The two proteins reacted in line with their amino content and solubility. The activation energy (E_a) of the amino group loss in the protein–glucose mixture was around 100 kJ per mol and that in the protein heated alone was higher. The E_a associated with the disappearance of glucose was around 90 kJ per mol. The E_a of UV absorbance and browning processes, which showed parallel time courses, were found to range from 90 to 150 kJ per mol.     

Influence of salt and pH on the solubility and structural characteristics of transglutaminase-treated wheat gluten hydrolysate

Hydrolyzed wheat gluten (GH, 77–85% protein) was prepared by limited chymotrypsin digestion at 37 °C for 4 h (degree of hydrolysis = 6.4%) and 15 h (degree of hydrolysis = 10.3%). Microbial transglutaminase (MTGase) treatment (55 °C for 1 h, or 5 °C for 18 h) effect on the solubility and structural characteristics of GH was examined under selected food processing conditions (pH 4.0–7.0, 0–0.6 M NaCl). The MTGase treatment increased solubility of GH by 3–29-fold (P < 0.05) within pH 4.0–7.0. Addition of 0.6 M NaCl or changing the conditions of MTGase incubation did not significantly alter solubility characteristics of GH. The MTGase treatment decreased surface hydrophobicity, and increased carboxyl groups in GH, suggesting cross-linking and deamidation. Fluorescence and UV spectra attributed the improved GH solubility to MTGase-induced polar environment, and partial masking of some nonpolar aromatic amino acids possibly due to high-molecular-weight polypeptides formed.     

The role of polyphenol oxidase and peroxidase in the browning of water caltrop pericarp during heat treatment

The mechanism of browning involving enzymatic browning was investigated in the pericarp of water caltrop, an Asian vegetable popular for its taste and medicinal properties. Polyphenol oxidase (PPO) and peroxidase (POD) activities were determined in pericarp at various times and temperatures. Water caltrop consisted of 44.22% moisture content, 37.23% crude fibre, and 2.63% crude protein. PPO and POD activities dropped from 62 and 38 units/g sample, respectively, as water temperature was increased from 30 to 80 °C. Optimum pH and temperature for PPO activity was at pH 5.0, 25–45 °C, and POD activity peaked at 60 °C. High PPO and POD activities at 40–50 °C resulted in degradation of phenolic compounds, which led to increased aggregation of browning pigments and discolouration (lower L-values) of the pericarp. Enzymatic browning was determined as the major factor in the browning discolouration of heat-treated water caltrop pericarp.     

Emulsifying properties of sweet potato protein: Effect of protein concentration and oil volume fraction

The effect of protein concentrations (0.1, 0.25, 0.5, 1.0, 1.5 and 2.0% w/v) and oil volume fractions (5, 15, 25, 35 and 45% v/v) on properties of stabilized emulsions of sweet potato proteins (SPPs) were investigated by use of the emulsifying activity index (EAI), emulsifying stability index (ESI), droplet size, rheological properties, interfacial properties and optical microscopy measurements at neutral pH. The protein concentration or oil volume fraction significantly affected droplet size, interfacial protein concentration, emulsion apparent viscosity, EAI and ESI. Increasing of protein concentration greatly decreased droplet size, EAI and apparent viscosity of SPP emulsions; however, there was a pronounced increase in ESI and interfacial protein concentration (P < 0.05). In contrast, increasing of oil volume fraction greatly increased droplet size, EAI and emulsion apparent viscosity of SPP emulsions, but decreased ESI and interfacial protein concentration significantly (P < 0.05). The rheological curve suggested that SPP emulsions were shear-thinning non-Newtonian fluids. Optical microscopy clearly demonstrated that droplet aggregates were formed at a lower protein concentration of <0.5% (w/v) due to low interfacial protein concentration, while at higher oil volume fractions of >25% (v/v) there was obvious coalescence. In addition, the main components of adsorbed SPP at the oil–water interface were Sporamin A, Sporamin B and some high-molecular-weight aggregates formed by disulfide linkage.     

Enzymatic hydrolysis of granular native and mildly heat-treated tapioca and sweet potato starches at sub-gelatinization temperature

The effect of mild heat treatment (below gelatinization temperature) towards the susceptibility of granular starch to enzymatic hydrolysis was investigated. Tapioca and sweet potato starches were subjected to enzymatic hydrolysis with a mixture of fungal α-amylase and glucoamylase at 35 °C for 24 h. Starches were hydrolyzed in native (granular) state and after heat treatment below gelatinization temperature (60 °C for 30 min). The dextrose equivalent (DE) value of heat-treated starch increased significantly compared to native starch, i.e., 36–50% and 27–34% for tapioca and sweet potato starch, respectively. Scanning electron microscopy examination showed that enzymatic erosion occurred mainly at the surface of starch granules. Hydrolyzed heat-treated starch exhibited rougher surface and porous granules compared to native starch. X-ray analysis suggested that enzymatic erosion preferentially occurred in amorphous areas of the granules. The amylose content, swelling power and solubility showed insignificant increase for both starches. Evidently, heating treatment below gelatinization temperature was effective in enhancing the degree of hydrolysis of granular starch.     

Characteristics and antioxidative activity of Maillard reaction products from a porcine plasma protein–glucose model system as influenced by pH

Maillard reaction products (MRPs) were prepared by heating the solution containing 2% porcine plasma protein (PPP) and 2% glucose adjusted to various pHs (8, 9, 10, 11 and 12) at 100 °C for different times (0, 2, 4, 6 and 8 h). The pH of all MRPs markedly decreased within 2 h of heating time. Browning and intermediate products, as monitored by absorbance at 420 nm and absorbance at 294 nm, sharply increased within 2 h (P < 0.05). Thereafter, slight increases were observed up to 8 h. Fluorescence intensity (Ex 347 and Em 415 nm) sharply increased within the first 2 h with a subsequent decrease when heating time increased (P < 0.05). Increases in browning and formation of intermediate products were concomitant with the decreases in free amino group and reducing sugar contents. Among all MRPs tested, those derived from the PPP–glucose system at pH 12 rendered the highest browning and intermediate products. However, no differences in reducing power or DPPH radical-scavenging activity of MRPs with initial pH ranges of 10–12 were noticeable. Electrophoretic study revealed that cross-linked proteins with high molecular weight were formed in the PPP–glucose model system to a greater extent at pHs 8 and 9, than at pHs 10–12. Nevertheless, heating times had no pronounced effect on protein pattern of glycated proteins.     

Functional properties of the Maillard reaction products of rice protein with sugar

The glycation of rice proteins with reducing sugars was investigated in an attempt to improve their solubility and functionality. Rice proteins isolated from a Chinese milled medium-grain rice were glycated with glucose, lactose, maltodextrin, or dextran in 2% aqueous dispersions. The sugar that provided the most improvement of the solubility, emulsification activity (EA) and emulsification stability (ES) of the Maillard reaction products was glucose. The optimum reaction conditions were at pH 11, 100 °C, and reaction time 15 min, which increased the solubility, EA and ES of rice protein from 20%, 0.46 and 11.1 to 92%, 0.64 and 18.2, respectively. Extending the reaction time beyond 15 min continued the development of latter-stage Maillard browning products without improvements in the functional properties of the Maillard reaction products. SEC–HPLC analysis with light scattering detection showed a decrease of the weight-averaged molecular weight from 500 to 100 K during the initial 15 min.     

Impact of dextran conjugation on physicochemical and gelling properties of sweet potato protein through Maillard reaction

Covalently linked sweet potato protein (SPP)–dextran conjugates were produced through Maillard reaction, and the effects of this conjugation on physicochemical and gelling properties of SPP were studied. Formation of SPP–dextran-conjugated product was confirmed with increase in browning intensity and molecular weight, with concomitant reduction in free amino group content of the protein. Dry-heating period of 0, 1, 3, 5 and 7 days gave rise to 0%, 12.8%, 19.0%, 25.2% and 22.8% degree of conjugation (DC), respectively. High molecular weight protein polymer with polydispersed band above 50 kDa was formed. FTIR spectroscopic analysis showed that the C-O (amide I) and C-N (amide II) stretching bands were modified by the Maillard reaction. Conjugation of SPP with dextran reduced its denaturation temperature. SPP–dextran conjugate gels’ network structures were sustained by both physical interactions and covalent bonds. SPP–dextran conjugates’ gels had significantly improved hardness and resilience in comparison with the unmodified SPP (P < 0.05).     

Amino acid composition of three species of Nigerian fish: Clarias anguillaris,Oreochromis niloticus and Cynoglossus senegalensis

An investigation into the concentrations of amino acids in three species of Nigerian fish: Clarias anguillaris, Oreochromis niloticus and Cynoglossus senegalensis was carried out. The most abundant amino acid was Glu (108–118 mg/g crude protein) and Leu was the most abundant essential amino acid (58.0–64.7 mg/g crude protein). While total amino acid content was 618–637 mg/g crude protein, the total essential amino acid content was 300–317 mg/g or 48.6–50.0% with His but 283–299 mg/g crude protein or 45.8–47.0% without His. The limiting amino acid was Thr for C. anguillaries and C. senegalensis but Val for O. niloticus whereas Phe + Tyr scores were greater than 1.0 (1.06–1.21) in all the fish samples. Significant differences existed between the contents of essential amino acids and non-essential amino acids at p < 0.05 in all the fish samples. Percentage contents of total neutral amino acids ranged from 52.2–54.9%; for total acidic amino acids the range was 26.9–29.6% and for total basic amino acids the range was 17.7–18.2%.     

Effect of reactant concentrations on the Maillard reaction in a fructose–glycine model system and the inhibition of black tiger shrimp polyphenoloxidase

The characteristics and the inhibitory activity towards black tiger shrimp polyphenoloxidase of Maillard reaction products (MRPs), prepared by heating an equimolar mixture of fructose and glycine at various concentrations (0.75–30 mM) at 100 °C for 12 h, were investigated. Increase in the intermediate products was observed with increasing reactant concentration, as evidenced by the increase in A₂₉₄ and fluorescence intensity. Furthermore, development of browning (A₄₂₀) was noticeable when the reactant concentration increased. The inhibitory activity of MRPs towards PPO gradually increased when the concentration of each reactant increased and reached a maximum at 30 mM (80% inhibition). The increase in the inhibitory activity of MRPs was coincidental with the increase in the reducing power, A₂₉₄, fluorescence intensity, as well as browning intensity. Generally, the development of Maillard reaction products was associated with decrease in pH and loss of reducing sugar and free amino groups, with coincidental increase in reducing power and copper-chelating property. MRPs with the reactant concentration of 4.5–30 mM were able to chelate the copper ion. Therefore, the inhibitory activity of MRPs towards browning, induced by PPO, was most likely due to their copper-chelating property as well as reducing power.     

Protein hydrolysates from meriga (Cirrhinus mrigala) egg and evaluation of their functional properties

Protein hydrolysates from underutilised meriga (Cirrhinus mrigala) fish egg were prepared by using commercial Alcalase and papain enzymes. The degree of hydrolysis was 62% for Alcalase and 17.1% for papain, after 90 min digestion at 50–55 and 60–65 °C, respectively. The protein content of Alcalase-produced hydrolysate was higher (85%) than that of papain hydrolysate (70%) (p < 0.05). Hydrolysis by both enzymes increased protein solubility of fish egg protein hydrolysates to above 72.4% over a wide pH range (2–12). Results showed that the hydrolysates had good fat absorption capacity (0.9 and 1.0 g/g sample), foam capacity (70% and 25%) and emulsifying capacity (4.25 and 5.98 ml/g hydrolysate), respectively for Alcalase and papain protein hydrolysates. Gel filtration chromatograms and SDS–PAGE analysis indicated the distribution of smaller peptides. These results suggested that fish egg protein hydrolysates could be useful in the food industry.     

Study of nonenzymic browning in α-amino acid and γ-aminobutyric acid/sugar model systems

The reactivities, in nonenzymic browning, of γ-aminobutyric acid (GABA), a non-protein amino acid with wide natural occurrence and potential health benefits as it occurs in foods, and of the α-l-amino acids arginine, glutamic acid, glutamine, leucine, lysine, and phenylalanine were investigated by heating equimolar mixtures of glucose and the cited amino acids at 110 °C at pH 6.0 for different times (0–4 h). Linear regression analysis indicated that the colour development in a GABA/glucose mixture was slower than that of a lysine/glucose mixture and comparable to that of a phenylalanine/glucose mixture. High-performance anion-exchange chromatography (HPAEC) with integrated pulsed amperometric detection (IPAD) showed that the decrease in GABA levels (ca. 10% after heating for 4 h) as a function of heating time was smaller than that of glucose (ca. 30% after heating for 4 h). At the same time, glucose to fructose isomerisation took place. After 20 min of heating at pH 6.0, all mixtures showed a fructose peak, the area of which increased with heating time. However, after correcting for fructose isomerisation, glucose losses were still higher than amino acid losses. In contrast to its precursor glutamic acid, GABA was stable during heating of a solution containing it alone. Heating of GABA-containing d-sugar solutions (xylose, fructose, glucose, maltose and sucrose) showed that the relative order of colour yield was pentose > hexose > disaccharides. As well as glucose to fructose isomerisation, HPAEC–IPAD allowed monitoring of the different isomerisation reactions occurring, and also disaccharide hydrolysis in the different GABA/sugar mixtures.     

Determination of cis- and trans- α- and β-carotenoids in Taiwanese sweet potatoes (Ipomoea batatas (L.) Lam.) harvested at various times

A HPLC method was improved to determine sweet potato carotenoids rapidly with good separation efficiency. A C30 column and a gradient solvent system consisting of methanol–acetonitrile–water (84/14/2, v/v/v, solvent A) and dichloromethane (solvent B) (a mixture of 80% A and 20% B was used initially, and then the mixing was programmed to 55% B within 15 min and kept to the end) were used for analysis. The flow rate was 1 ml/min and detection was at 450 nm. A total of 11 all-trans and cis forms of α- and β-carotene in Taiwanese sweet potato (Ipomoea batatas (L.) Lam.) could be resolved within 16 min. The orange-fleshed sweet potato (Tainung 66) had higher total carotenoid content than the yellow-fleshed one (Tainung 57) at the same harvest time. The total carotenoid levels in both crops harvested at various times were in the order: October > July > April > January.     

Polyphenol oxidase activity,phenolic acid composition and browning in cashew apple (Anacardium occidentale, L.) after processing

This study describes the extraction and characterisation of cashew apple polyphenol oxidase (PPO) and the effect of wounding on cashew apple phenolic acid composition, PPO activity and fruit browning. Purification factor was 59 at 95% (NH₄)₂SO₄ saturation. For PPO activity, the optimal substrate was catechol and the optimum pH was 6.5. PPO K_m and V_max values were 18.8 mM and 13.6 U min⁻¹ ml⁻¹, respectively. Ascorbic acid, citric acid, sodium sulphite and sodium metabisulphite decreased PPO activity, while sodium chloride increased PPO activity. Wounding at 2 °C and 27 °C for 24 h increased PPO activity but storage at 40 °C reduced PPO activity. Gallic acid, protocatechuic acid and cinnamic acid (free and conjugate) were identified in cashew apple juice. Cutting and subsequent storage at 40 °C hydrolysed cinnamic acid. 5-Hydroxymethylfurfural content in cashew apple juice increased after injury and storage at higher temperatures, indicating non-enzymatic browning.     

Extraction and characterisation of pepsin-solubilised collagen from the skin of unicorn leatherjacket (Aluterus monocerous)

Pepsin-solubilised collagen (PSC) was extracted from the skin of unicorn leatherjacket (Aluterus monocerous), using 0.5 M acetic acid in the presence of pepsin from albacore tuna, yellowfin tuna or porcine pepsin at a level of 20 units/g of defatted skin. Yields of 8.48 ± 0.3%, 8.40 ± 0.3% and 7.56 ± 0.4% (wet weight basis) were obtained for PSC extracted with the aid of albacore tuna pepsin (APSC), yellowfin tuna pepsin (YPSC) and porcine pepsin (PPSC), respectively. All PSCs were classified as Type I collagen containing two α₁-chains and one α₂-chain with no disulphide bond. The peptide maps of different PSCs hydrolysed by V8 protease and lysyl endopeptidase were different. ATR-FTIR spectra analysis revealed that PSC molecules had the compact triple helical structure stabilised mainly by the hydrogen bond. T_max of all PSCs (31.68–31.98 °C) shifted to lower values (29.33–29.40 °C) when dispersed in 0.05 M acetic acid, indicating the conformational changes in the collagen structure induced by acid. Relative viscosity of 0.03% PSC in 0.1 M acetic acid solution decreased progressively as the temperature increased from 4 to 52 °C, indicating thermal destabilisation or denaturation of PSC molecules. All PSCs were soluble in the pH range of 1–6 and sharply decreased at neutral pH. Decreases in solubility were observed in the presence of NaCl, especially at concentrations above 2% (w/v). Therefore, the skin of unicorn leatherjacket could serve as a potential source of collagen.     

Efficacy of sodium chlorite as an inhibitor of enzymatic browning in apple slices

Sodium chlorite (SC) is an effective sanitizer for inhibiting microbial growth. This investigation was conducted to determine the efficacy of SC as a browning control agent for use on fresh-cut apple slices, applied alone, or in conjunction with organic acids. Additionally, the authors compared the efficacy of SC to that of acidified sodium chlorite (ASC) and to several other salts and examined the effect of pH and several different organic acids on efficacy of SC. The fresh-cut apple slices were dipped in treatment solutions for 1 min, then drained and placed in plastic containers at 20 °C for 24 h, and finally stored in polyethylene bags at 5 °C for 2 weeks. Color was measured periodically during storage. Lightness (L) values for all treated and control samples measured at 4 h, 24 h, and 2 weeks of storage were compared to L value for untreated samples measured immediately after cutting. Percent decrease in L-values was calculated for each sample at each time interval. Apple slices treated in ASC or SC solution had a significantly smaller decrease in L value indicating less browning than those treated in citric acid or water control at 4 h (P < 0.01), and with the exception of 1 g L⁻¹ ASC and 0.1 g L⁻¹ SC, all other ASC and SC treated slices still had significantly less browning than those for the water control (P < 0.01) at 24 h. After 2 weeks of storage, only SC (0.5–1.0 g L⁻¹), sodium bisulfite (0.5 g L⁻¹) and calcium l-ascorbate (10 g L⁻¹) continued to inhibit browning. Treatment with 0.5 g L⁻¹ SC and pH adjusted in the range from 3.9 to 6.2 using citric acid (CA) reduced browning more effectively than 0.5 g L⁻¹ SC without pH adjustment. Two organic acids, salicylic acid and cinnamic acid, when added to SC solution, were found to achieve even better inhibition of browning than CA at the same pH value.     

Biochemical properties of two isoforms of trypsin purified from the Intestine of skipjack tuna (Katsuwonus pelamis)

Two trypsins (A and B) from the intestine of skipjack tuna (Katsuwonus pelamis) were purified by Sephacryl S-200, Sephadex G-50 and DEAE-cellulose with a 177- and 257-fold increase in specific activity and 23% and 21% recovery for trypsin A and B, respectively. Purified trypsins revealed a single band on native-PAGE. The molecular weights of both trypsins were 24 kDa as estimated by size exclusion chromatography and SDS–PAGE. Trypsin A and B exhibited the maximal activity at 55 °C and 60 °C, respectively, and had the same optimal pH at 9.0. Both trypsins were stable up to 50 °C and in the pH range from 6.0 to 11.0. Both trypsin A and B were stabilised by calcium ion. Activity of both trypsins continuously decreased with increasing NaCl concentration (0–30%) and were inhibited by the specific trypsin inhibitors – soybean trypsin inhibitor and N-p-tosyl-l-lysine chloromethyl ketone. Apparent K_m and K_cat of trypsin A and B were 0.22–0.31 mM and 69.5–82.5 S⁻¹, respectively. The N-terminal amino acid sequences of the first 20 amino acids of trypsin A and B were IVGGYECQAHSQPPQVSLNA and IVGGYECQAHSQPPQVSLNS, respectively.     

Kinetics of enthalpy relaxation of milk protein concentrate powder upon ageing and its effect on solubility

Kinetics of enthalpy relaxation of milk protein concentrate (MPC) powder upon short-term (up to 67 h) storage at 25 °C and a_w 0.85, and long-term (up to 48 days) storage at 25 °C and a range of a_w values (0–0.85) were studied by differential scanning calorimetry (DSC). The short-term study showed a rapid recovery of enthalpy for the first 48 h, followed by a slower steady increase with time. The non-exponential β parameter was calculated using the Kohlrausch–Williams–Watts function and found to be 0.39. Long-term storage showed that enthalpy relaxation depends on both storage period and water activity. The enthalpy value was much less for lower moisture content (mc) (a_w ? 0.23, mc ? 5.5%) than for higher mc (a_w ? 0.45, mc ? 8%) samples for a particular storage period. The results suggest that the presence of more water molecules, in close proximity to the protein surface facilitates kinetic unfreezing and subsequent motion of molecular segments of protein molecules towards thermodynamic equilibrium. Although de-ageing of stored samples did not reverse storage-induced solubility losses, the timescale of enthalpy relaxation was similar to that of solubility loss. It is suggested that enthalpy relaxation within stored samples allows structural rearrangements that are responsible for subsequent solubility decreases.