Effects of plasticizers on the properties of edible films from skin gelatin of bigeye snapper and brownstripe red snapper

The effects of type and concentration of plasticizers on the mechanical properties (tensile strength, TS and elongation at break, EAB), water vapor permeability, light transmission, transparency and color of fish skin gelatin edible films from bigeye snapper (Priacanthus marcracanthus) and brownstripe red snapper (Lutjanus vitta) were investigated. At the same plasticizer concentration, fish skin gelatin films from both species plasticized with glycerol (Gly) showed the greatest EAB (P<0.05), whereas ethylene glycol (EG) plasticized films showed the highest TS (P<0.05). Films prepared from brownstripe red snapper skin gelatin exhibited slightly greater TS than those of bigeye snapper skin gelatin (P<0.05) when Gly and sorbitol (Sor) were used. EG, polyethylene glycol 200 (PEG 200) and polyethylene glycol 400 (PEG 400) affected the mechanical properties of both films differently. Films generally became more transparent and EAB, water vapor permeability (WVP), as well as light transmission of films increased, but TS and yellowness decreased with increasing plasticizer concentrations.     

Skin gelatin from bigeye snapper and brownstripe red snapper: Chemical compositions and effect of microbial transglutaminase on gel properties

Fish skin gelatin was extracted from the skin of bigeye snapper (Priacanthus macracanthus) and brownstripe red snapper (Lutjanus vitta) with yields of 6.5% and 9.4% on the basis of wet weight, respectively. Both skin gelatins having high protein but low fat content contained high hydroxyproline content (75.0 and 71.5 mg/g gelatin powder). The bloom strength of gelatin gel from brownstripe red snapper skin gelatin (218.6 g) was greater than that of bigeye snapper skin gelatin (105.7 g) (P<0.05). The addition of microbial transglutaminase (MTGase) at concentrations up to 0.005% and 0.01% (w/v) increased the bloom strength of gelatin gel from bigeye snapper and brownstripe red snapper, respectively (P<0.05). However, the bloom strength of skin gelatin gel from both fish species decreased with further increase in MTGase concentration. SDS-PAGE of gelatin gel added with MTGase showed the decrease in band intensity of protein components, especially, β- and γ- components, suggesting the cross-linking of these components induced by MTGase. Microstructure studies revealed that denser and finer structure was observed with the addition of MTGase.     

Isolation and characterization of collagen from bigeye snapper (Priacanthus macracanthus) skin

Acid‐solubilized collagen (ASC) and pepsin‐solubilized collagen (PSC) were isolated from the skin of bigeye snapper (Priacanthus macracanthus) with yields of 64 and 11 g kg^?1 wet weight, respectively. Both ASC and PSC were characterized as type I collagens with no disulfide bonds. Peptide maps of ASC and PSC digested by V8 protease and lysyl endopeptidase showed some differences in peptide patterns and were totally different from those of calf skin collagen. The maximum solubility was observed at pH 4 and 5 for ASC and PSC, respectively. A sharp decrease in solubility of both collagens in acetic acid was found with NaCl concentration above 30 g l^?1. Thermal transitions of ASC and PSC in deionized water were observed with T_max of 30.37 and 30.87 °C, respectively, and were lowered in the presence of acetic acid (0.05 mol kg^?1 solution). Therefore, ASC was a major fraction in bigeye snapper skin and it exhibited some different characteristics to PSC. Copyright © 2005 Society of Chemical Industry     

Effect of irradiation on properties and storage stability of Som-fug produced from bigeye snapper

Effects of irradiation at different doses (0, 2 and 6 kilogray (kGy)) on the microbiological, chemical and physical properties of Som-fug, a Thai fermented fish mince, were investigated. Lactic acid bacteria (LAB), yeast and mould counts in samples irradiated at 6 kGy were not detectable throughout the storage of 30 days at 4 °C, whereas no growth was found in the sample irradiated at 2 kGy within the first 10 days. Generally, greater carbonyl contents of lipid and protein, as well as thiobarbituric acid-reactive substances (TBARS), were noticeable in the irradiated samples, than in the non-irradiated sample (p < 0.05). The carbonyl contents and TBARS increased with increasing storage time and the rate of increase was more pronounced in samples irradiated at higher dose (p < 0.05). With increasing storage time, Som-fug irradiated at 6 kGy showed greater decreases in hardness, adhesiveness, springiness and cohesiveness, than did non-irradiated samples and those irradiated at 2 kGy (p < 0.05). L^∗ value of all samples decreased, whereas a^∗ and b^∗ values increased throughout storage (p < 0.05). Lower acceptance in all attributes was observed in the samples irradiated at 6 kGy, than in other samples, particularly when storage time increased (p < 0.05). However, samples irradiated at 2 kGy showed no changes in acceptability within 20 days. The results revealed that irradiation at high dose (6 kGy) might induce lipid and protein oxidation, though the growth of microorganisms was inhibited. Therefore, the irradiation at low dose (2 kGy) could be used to control the overfermentation of Som-fug up to 20 days at 4 °C without adverse effects on quality and acceptability.     

Porcine plasma protein as proteinase inhibitor in bigeye snapper (Priacanthus tayenus) muscle and surimi

Porcine plasma protein (PPP) showed inhibitory activity towards trypsin, papain, digestive enzymes and modori‐inducing proteinases from bigeye snapper. Among the fractions prepared, fraction IV‐1 exhibited the highest inhibitory activity against all proteinases tested and the autolysis of fish muscle. At a level of 0.5% (w/w), both PPP and fraction IV‐1 effectively prevented the degradation of myosin heavy chain in fish muscle. The inhibitory activity of fraction IV‐1 was stable up to 60 °C. Incorporation of fraction IV‐1 significantly increased the breaking force, deformation and water‐holding capacity of surimi gel from bigeye snapper (P < 0.05). However, no increase in breaking force and deformation was found when fraction IV‐1 was added at a level above 0.3% (w/w) (P > 0.05). No significant change in whiteness of surimi gel was observed with the addition of fraction IV‐1 (P > 0.05). © 2001 Society of Chemical Industry     

Cross-linking activity of sarcoplasmic fraction from bigeye snapper (Priacanthus tayenus) muscle

Addition of sarcoplasmic fraction from bigeye snapper (Priacanthus tayenus) into natural actomyosin in combination with setting at 40°C resulted in the cross-linking of myosin heavy chain (MHC). Higher amount of sarcoplasmic fraction and extended setting time resulted in a higher cross-linking, indicating the presence of endogenous transglutaminase (TGase) in bigeye snapper muscle. TGase activity was activated by calcium ion and reducing agents (β-mercaptoethanol and dithiotreitol), but was inhibited by N-ethylmaleimide (NEM), NH₄Cl and EDTA. TGase in the sarcoplasmic fraction was not stable when heated at temperature above 40°C, particularly with an increasing heating time. TGase was stable at pH ranging from 5.0 to 7.0, in which more than 70% activity was retained. Therefore, sarcoplasmic fraction possessed a cross-linking activity caused by TGase and its recovery for further uses should be considered.     

Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus)

The compositions and some properties of acid-soluble collagens (ASC) of the skin and bone of bigeye snapper, (Priacanthus tayenus) were investigated. The collagens were extracted with the yields of 10.94% and 1.59% on the basis of wet weight, from skin and bone, respectively. Similar electrophoretic patterns of collagens from the skin and bone were observed. Both collagens comprised two different α chains, α1 and α2 and were classified as type I collagen. However, peptide maps of collagen from the skin and bone of bigeye snapper, digested by V8 protease and lysyl endopeptidase, revealed differences between collagens from skin and bone, and both were completely different from those of calf skin collagen. Collagen rehydrated in acetic acid had lower T_max and enthalpy than those rehydrated in deionised water, suggesting a conformational change caused by acid. Collagens form the skin and bone had the highest solubility at pH 2 and 5, respectively. No changes in solubility were observed in the presence of NaCl up to 3% (w/v). However, a sharp decrease in solubility was found with NaCl above 3% (w/v).     

Impact of lecithin incorporation on gel properties of bigeye snapper (Priacanthus tayenus) surimi

Gelling characteristics of bigeye snapper (Priacanthus tayenus) surimi functionalised by lecithin at different concentrations were investigated. Lecithin at ≤1 g 100 g⁻¹ had no impact on breaking force and deformation (P > 0.05). Expressible drip tended to decrease with increasing lecithin level up to 1 g 100 g⁻¹. Lecithin at 1–3 g 100 g⁻¹ improved the whiteness (P < 0.05). Jointed clusters were formed in the gel microstructure with 1 g 100 g⁻¹ lecithin. Gel without and with 1 g 100 g⁻¹ lecithin had the same texture profile and likeness scores (texture, odour and flavour) (P > 0.05). Peroxide value, TBARS content and rancid odour score of gels were changed considerably during refrigerated storage (4 °C/polyethylene bag) for 15 days but lower values of all indices were noticeable in gel with lecithin. Therefore, lecithin at 1 g 100 g⁻¹ was the optimum concentration for stabilising the texture, improving the water holding capacity, whitening the colour and retarding the lipid oxidation of bigeye snapper surimi gel.     

Comparative study on proteolysis of two species of bigeye snapper,Priacanthus macracanthus and Priacanthus tayenus

Proteolytic activity in muscle from two species of bigeye snapper (Priacanthus macracanthus and Priacanthus tayenus) was studied. Autolysis of mince and washed mince at 50 and 60 °C was compared. Higher degradation of myosin heavy chain was observed in both mince and washed mince from P macracanthus than in those from P tayenus, especially when the incubation time was increased. Autolysis of washed mince from both species was inhibited by soybean trypsin inhibitor, suggesting that myofibril‐associated proteases were serine proteases. When sarcoplasmic proteolytic activity in P macracanthus muscle was studied, two activity peaks with an optimum temperature of 60 °C were observed at pH 6.5 and 8.5. The activities of both peaks were mostly inhibited by soybean trypsin inhibitor, suggesting that the major protease was a serine protease. Major sarcoplasmic proteolytic activity in P macracanthus muscle was found at M_r 62 000 on sodium dodecyl sulphate substrate gel. For P tayenus sarcoplasmic proteolytic activity, two activity peaks with an optimum temperature of 60 °C were found at pH 5.0 and 8.5. The pH 5.0 peak activity was effectively inhibited by pepstatin A, while the pH 8.5 peak activity was inhibited by several inhibitors. The results indicated that various sarcoplasmic proteases were present in P tayenus muscle. The two species contained different sarcoplasmic proteases in terms of composition and activity level. P macracanthus muscle generally had higher sarcoplasmic proteolytic activities than P tayenus muscle. Copyright © 2003 Society of Chemical Industry     

Functional properties of pH-shifted protein isolates from bigeye snapper (Priacanthus tayenus) head by-product

The functional properties of pH-shifted protein isolates from bigeye snapper head were evaluated. Alkaline isolate showed a superior salt-solubility and gel forming ability to acid counterpart as indicated by a regular gel structure (i.e., imaged by scanning electron microscope) with higher gel strength and lower expressible drip (p < 0.05). Acid isolate exhibited higher surface hydrophobicity (p < 0.05) and thereby improved interfacial properties. Emulsifying activity index of acid isolate was lower than commercial whey protein and egg-white (p < 0.05) but its emulsion stability was better (p < 0.05). Both protein isolates had lower foamability than commercial proteins but their foam stability was not different (p > 0.05).     

Use of pepsin for collagen extraction from the skin of bigeye snapper (Priacanthus tayenus)

Extraction and some properties of pepsin-solubilised collagens from the skin of bigeye snapper (Priacanthus tayenus) were investigated. Addition of bigeye snapper pepsin (BSP) at a level of 20 kUnits/g of defatted skin resulted in an increased content of collagen extracted from bigeye snapper skin. The yields of collagen from bigeye snapper skin extracted for 48 h with acid and with BSP were 5.31% and 18.74% (dry basis), respectively. With pre-swelling in acid for 24 h, collagen extracted with BSP at a level of 20 kUnits/g of defatted skin for 48 h had a yield of 19.79%, which was greater than that of collagen extracted using porcine pepsin at the same level (13.03%). The skin collagen was characterised to be type I with no disulfide bond. Electrophoretic study revealed slight differences in molecular weight between acid-solubilised collagen and all pepsin-solubilised collagens. The molecular weights of α1 and α2 chains in acid-solubilised collagen were estimated to be 120 and 112 kDa, respectively, whereas α1 and α2 chains of pepsin-solubilised collagens had molecular weights of 118 and 111 kDa, respectively. The result suggested that these pepsin-solubilised collagens might undergo partial cleavage in the telopeptide region by pepsin treatment. The maximum transition temperature (T_max) of acid-solubilised collagen was observed at 32.5 °C, which was slightly higher than that of pepsin-solubilised collagens (by about 1 °C). Generally, all collagens were highly solubilised in the pH range of 2–5 and sharply decreased at the neutral pH. No changes in solubility were observed in the presence of NaCl up to 3% (w/v) and the decrease was more pronounced with increasing NaCl concentration.     

Enhancement of gel strength of bigeye snapper (Priacanthus tayenus) surimi using oxidised phenolic compounds

Effects of different oxidised phenolic compounds (ferulic acid, OFA; tannic acid, OTA; catechin, OCT and caffeic acid, OCF) at different levels (0–0.25% of protein content) on the properties of gels from bigeye snapper (Priacanthus tayenus) surimi were investigated. Breaking force and deformation of surimi gel varied with types and amounts of oxidised phenolic compounds. Gels added with 0.20% OFA, 0.05% OTA, 0.15% OCF and 0.05% OCT exhibited the marked increases in both breaking force and deformation, compared with the control (P < 0.05). Those increases were associated with lower expressible moisture content. No increases in both breaking force and deformation were observed when ferulic acid without oxygenation at alkaline pH was added, regardless of amount added (P > 0.05). No changes in the whiteness of gel were found with addition of OFA (P > 0.05), but the decreases in whiteness were noticeable as other oxidised phenolics were incorporated (P < 0.05). Different microstructures were obtained among gels with different oxidised phenolics. The physicochemical properties of natural actomyosin suggest that oxidised phenolics could induce conformational changes and the cross-linking through amino groups or the induction of disulphide bond formation. Therefore, the addition of oxidised phenolic compounds at the optimum level could increase the gel strength of surimi gel.     

Effect of phosphate compounds on gel-forming ability of surimi from bigeye snapper (Priacanthus tayenus)

The properties of surimi gel from bigeye snapper (Priacanthus tayenus) added with various phosphate compounds (sodium pyrophosphate, PP; sodium tripolyphosphate, TPP; and sodium hexametaphosphate, HMP) at different levels (0%, 0.05%, 0.1%, 0.3% and 0.5% w/w) and heated under various conditions were studied. Kamaboko and directly heated gels from bigeye snapper surimi added with 0.05% PP had the increase in breaking force and deformation by 17.35% and 11.52%, and 13.54% and 3.53%, respectively, compared with the control gel (without PP addition). At the same level used (0.05%), TPP had no influence, but HMP exhibited a detrimental effect on kamaboko gel. The addition of PP (0.025%) in combination with 50 mmol CaCl₂/kg increased the breaking force by 38.68% as compared with the control gel (without additives), suggesting that the sufficient amount of CaCl₂ could enhance the setting of the gel. Generally, the marked decrease in breaking force with the coincidental increased expressible moisture was observed when the excessive amount of phosphate compounds was used (p<0.05). Microstructure study revealed that a gel with a fine network was formed with addition of PP. Therefore, the addition of PP in combination with CaCl₂ could increase the gel strength as well as water holding capacity of surimi gel.     

Characteristics of gelatin from the skins of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus

Gelatins extracted from the skins containing fine scales of two species of bigeye snapper, Priacanthus tayenus (GT) and Priacanthus macracanthus (GM), were characterised. Both gelatins had the protein as the major component with high content of imino acids (proline & hydroxyproline) (186.29–187.42 mg/g). GT and GM contained calcium at levels of 6.53 and 2.92 g/kg, respectively. Both gelatins contained α1 and α2 chains as the predominant components and some degradation peptides. The absorption bands of both gelatins in Fourier transform infrared (FTIR) spectra were mainly situated in the amide band region (amide I and amide II). GT and GM had a relative solubility greater than 90% in the wide pH ranges (1–10). The bloom strength of GM (254.10 g) was higher than that of GT (227.73 g) (P < 0.05), but was slightly lower than that of commercial bovine gelatin (293.22 g) (P < 0.05). Finer gel structure with smaller strands and voids was observed in GM gel, in comparison with that observed in GT counterpart.     

Gel‐forming properties of surimi produced from bigeye snapper,Priacanthus tayenus and P macracanthus,stored in ice

The influence of iced storage of two species of bigeye snapper, Priacanthus tayenus and P macracanthus, on the gel‐forming ability of the resulting surimi was investigated. Upon iced storage, whole fish underwent deterioration faster than beheaded/eviscerated fish. Total volatile base and trimethylamine contents of whole fish were higher than those of beheaded/eviscerated fish, particularly after 9 days of storage (P < 0.05). P macracanthus muscle was more susceptible to proteolytic degradation than P tayenus muscle. Ca²⁺‐ATPase activity decreased as the storage time increased (P < 0.05), indicating the denaturation of myosin. A marked decrease in Ca²⁺‐ATPase activity was found in whole fish kept for more than 6 days in ice (P < 0.05). Breaking force and deformation of surimi gels from both species decreased, with a concomitant decrease in whiteness, as the storage time increased (P < 0.05). Beheading and evisceration of fish retarded the deterioration. However, the gel‐forming ability of surimi produced from both species decreased continuously throughout iced storage (P < 0.05), probably owing to the denaturation and degradation of myofibrillar proteins. © 2002 Society of Chemical Industry     

Extraction and characterisation of pepsin‐solubilised collagens from the skin of bigeye snapper (Priacanthus tayenus and Priacanthus macracanthus)

BACKGROUND: Fish collagen has been paid increasing attention as an alternative to the mammalian counterpart owing to the abundance of fish skin as a processing by‐product. Generally, the low yield of collagen extracted using the typical acid solubilisation process has led to the use of mammalian pepsin as an aid for increasing the yield. Alternatively, fish pepsin, especially from tuna stomach, can be used for the extraction of pepsin‐solubilised collagen (PSC). Therefore the objective of this study was to extract and characterise PSC from the skin of bigeye snapper, a fish widely used for surimi production in Thailand. RESULTS: PSCs from the skin of two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus, were extracted with the aid of tongol tuna (Thunnus tonggol) pepsin and porcine pepsin. PSCs from the skin of both species extracted using porcine pepsin had a higher content of β‐chain but a lower content of α‐chains compared with those extracted using tuna pepsin. All PSCs contained glycine as the major amino acid and had an imino acid (proline and hydroxyproline) content of 189–193 residues per 1000 residues. Transition temperatures of PSCs were in the range 30.6–31.3 °C. Fourier transform infrared spectra revealed some differences in molecular order between PSCs extracted using porcine pepsin and tuna pepsin. Nevertheless, the triple‐helical structure of PSCs was not affected by pepsin digestion. Zeta potential analysis indicated that PSCs from P. tayens and P. macracanthus possessed zero net charge at pH 7.15–7.46 and 5.97–6.44 respectively. CONCLUSION: Tongol tuna pepsin could be used as a replacement for mammalian pepsin in PSC extraction. However, a slight difference in PSC properties was found. Copyright © 2009 Society of Chemical Industry     

Effect of microbial transglutaminase on rheological properties of oxidised and non‐oxidised natural actomyosin from two species of bigeye snapper

The contribution of microbial transglutaminase (MTGase) to the thermal gelation of non‐oxidised and oxidised natural actomyosin (NAM) from two species of bigeye snapper was studied by dynamic rheological testing. Under two‐step heating, the addition of MTGase increased the gel‐forming ability of both species. During setting at 40 °C, Priacanthus macracanthus NAM seemed to show higher reactivity to MTGase than P tayenus NAM, resulting in a higher rate and magnitude of G′ development. An increase in final G′ of NAM from P macracanthus and P tayenus by 13.7–24 and 6.6–10.8 times respectively was observed compared with NAM alone. Iron‐catalysed oxidation substantially decreased the gel‐forming ability of P tayenus NAM but enhanced that of P macracanthus NAM. However, oxidation decreased the reactivity of both NAM types to added MTGase. The results suggested that the native NAM structure was essential for MTGase to maximise the setting response. The gel‐forming ability and setting response of denatured NAM were partially recovered by the addition of MTGase. © 2002 Society of Chemical Industry     

Use of pyloric caeca extract from bigeye snapper (Priacanthus macracanthus) for the production of gelatin hydrolysate with antioxidative activity

Proteolytic activity of pyloric caeca extract (PCE) from bigeye snapper (Priacanthus macracanthus) was studied. The highest activity was observed at 55 °C and pH 8.0 when casein, N^α-Benzoyl-dl-arginine-p-nitroanilide (BAPNA) and N^α-p-Tosyl-l-arginine methyl ester hydrochloride (TAME) were used as the substrates. The activity was inhibited markedly by 1 mg/ml soybean trypsin inhibitor, whereas E-64, pepstatin A and EDTA exhibited a negligible effect on activity. The results suggested that a trypsin-like enzyme was most likely the major proteinase in PCE. As determined by activity staining, two proteolytic activity bands with apparent molecular weights of 55 and 24 kDa were found. Gelatin hydrolysate from bigeye snapper skin prepared using PCE exhibited the increases in 2,2-Diphenyl-1-picrylhydrazyl (DPPH), 2,2-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activities and ferric reducing antioxidative power (FRAP) as degrees of hydrolysis (DHs) increased (P < 0.05). Hydrolysates derived from gelatin using Alcalase combined with PCE showed the highest ABTS radical scavenging activity (P < 0.05). Gelatin hydrolysate prepared using Alcalase in combination with Neutrase or PCE at 500 and 1000 ppm, respectively, retarded the oxidation in both linoleic acid oxidation and lecithin liposome oxidation systems. The antioxidative peptide of gelatin hydrolysate had a molecular weight of 1.7 kDa.     

New developments in manufacturing of Surimi and Surimi seafood

Abstract

Manufacturing technology of surimi and surimi seafood has been developed to keep the balance of the quality and quantity (yield) of surimi proteins. This review article covers the chemistry of surimi manufacturing with an emphasis on solubility of myofibrillar proteins as affected by ionic strength, pH, washing cycles, wash/meat (W/M) ratio, and proteolysis. In addition, water quality, waste water, and cryoprotection are reviewed. Ohmic heating and high hydrostatic pressure in relation to the manufacturing of surimi seafood are extensively discussed. Ohmic heating is the newest technology applied in the manufacturing of surimi seafood. High hydrostatic pressure has not been applied in the commercial practices of surimi seafood manufacturing, however, it has a great potential to make surimi gels stronger.     

Cryoprotectant Effects in Surimi and Surimi/Mince-based Extruded Products

The relative cryoprotective effects of liquid sorbitol (L) alone and in combination with sucrose (L-S) was assessed in surimi, extruded uncooked and cooked products, and compared with the cryoprotective effects of crystalline sorbitol (C), liquid polyol (P), and modified starch (MS). Variables evaluated included gel-forming properties, cooking loss, drip loss and ice crystal formation. Addition of 8% sorbitol resulted in best water-holding ability, gel strength and least ice crystal formation. A better cryoprotective effect was shown in uncooked than in cooked products. No significant differences in effectiveness were found among C, C-S, L and L-S. Optimum sweetness was obtained with either C and L at 8% or L-S at 3:3%. Both C-S and L-S at 4:4% were judged to be slightly too sweet.