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     

Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish

Effects of setting at 25 °C on textural properties and cross-linking of myofibrillar proteins in surimi produced from threadfin bream (Nemipterus bleekeri), bigeye snapper (Priacanthus tayenus), barracuda (Sphyraena jello) and bigeye croaker (Pennahai macrophthalmus) were investigated. Increase in setting time (0–8 h) resulted in a higher breaking force and deformation for all surimi gels tested (P<0.05). Increased gel strength was associated with increase in non-disulfide bond formation and decreased heavy chain myosin. Proteins underwent degradation during setting; however polymerization occurred to a much higher extent, leading to a strengthened gel matrix. Therefore, setting at 25 °C, for an appropriate time, should be a promising means to improve gelling properties of surimi produced from tropical fish.     

GEL PROPERTIES OF BIGEYE SNAPPER (PRIACANTHUS TAYENUS) SURIMI AS AFFECTED BY SETTING AND PORCINE PLASMA PROTEINS

Effects of setting temperature, time, and addition of porcine plasma protein (PPP) on gel properties of surimi from bigeye snapper (Priacanthus tayenus) were investigated. Breaking force and deformation of the surimi gels increased as the setting time and temperature increased. The gel preincubated at 35C for 90 min in the presence of 0.5% PPP, followed by cooking at 90C for 20 min showed the maximum force and deformation. The decrease in solubility of the resultant suwari and kamaboko gels in solution containing sodium dodecyl sulfate, urea and β‐mercaptoethanol suggested that gel enhancement was mainly mediated through the formation of nondisulfide covalent bonds catalyzed by both transglutaminase (TGase) in fish muscle and porcine plasma. Addition of PPP slightly decreased the whiteness of the kamaboko gels.     

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.     

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     

Effect of high-temperature setting on gelling characteristic of surimi from some tropical fish

The effect of setting at 40 °C on the textural properties and the changes in myofibrillar proteins in surimi produced from threadfin bream (Nemipterus bleekeri), bigeye snapper (Priacanthus tayenus), barracuda (Sphyraena jello) and bigeye croaker (Pennahai macrophthalmus) was investigated. An increase in the time of setting generally resulted in higher breaking force and also the deformation of both suwari and kamaboko gels. Maximum increases in gel‐breaking force were obtained in 1 h for threadfin bream, 2 h for bigeye snapper, 1.5 h for barracuda and 3 h for bigeye croaker. Extended setting time caused decreases in breaking force and deformation in all surimi, except that produced from bigeye croaker. Gel strengthening was associated with an increase in non‐disulphide covalent bond formation. Degradation of proteins occurred with prolonged setting. Therefore, setting at 40 °C for an appropriate time is a promising means to improve the gelling property of surimi produced from tropical fish.     

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     

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.     

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.     

Effect of porcine plasma protein and setting on gel properties of surimi produced from fish caught in Thailand

Effects of porcine plasma protein (PPP) and high temperature setting on gel properties of surimi from bigeye snapper, bigeye croaker, threadfin bream and barracuda were investigated. PPP was effective in increasing breaking force and deformation of kamaboko gels set at 40°C for 30 min and heated at 90°C for 20 min. The optimum levels of PPP were 0.5, 0.5, 1.5 and 1.5 g/100 g and the optimum setting times were 2, 1.5, 1.5 and 2 h for bigeye snapper, bigeye croaker, threadfin bream and barracuda surimi, respectively. However, the addition of PPP significantly decreased whiteness (P<0.05). An increase in gel-forming ability of surimi with PPP coincided with a decrease in solubility in mixture of SDS, urea and β-mercaptoethanol, indicating the formation of nondisulfide covalent bond induced by both endogenous and plasma transglutaminase. The results supported that PPP improve the gelation of surimi in combination with setting.     

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.     

Whey protein concentrate: Autolysis inhibition and effects on the gel properties of surimi prepared from tropical fish

Effects of whey protein concentrate (WPC) on autolysis inhibition and gel properties of surimi produced from bigeye snapper (Priacanthus tayenus), goatfish (Mulloidichthys vanicolensis), threadfin bream (Nemipterus bleekeri) and lizardfish (Saurida tumbil) were investigated. WPC (0–3%) showed inhibitory activity against autolysis in all surimi at both 60 and 65 °C in a concentration-dependent manner. Myosin heavy chain (MHC) of surimi was more retained in the presence of WPC. Breaking force and deformation of kamaboko gels of all surimi increased as added levels of WPC increased (P < 0.05). This was associated with lower levels of protein degradation, as evidenced by the decrease in trichloroacetic acid-soluble peptide content (P < 0.05). WPC at 3% (w/w) significantly decreased the whiteness of gels. However, water-holding capacity of kamaboko gels was improved with increasing concentration of WPC. The microstructure of surimi gels generally became denser with the addition of WPC.     

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.     

Purification and characterisation of transglutaminase from four fish species: Effect of added transglutaminase on the viscoelastic behaviour of fish mince

The transglutaminase (TGase) enzyme from four different fish species, namely bigeye snapper, Indian oil sardine, tilapia and common carp have been isolated and characterised. The specific activity of the enzyme was higher in tilapia followed by oil sardine, common carp and bigeye snapper. The molecular weight of pure TGase was found to be in the range of 73–95 kD for four different fish species. The temperature optima for maximum activity of TGase varied amongst four species studied. The effect of activator (calcium chloride) and inhibitors (ethylenediaminetetraacetic acid (EDTA), ammonium chloride and free lysine–hydrochloride) at different concentrations on the TGase enzyme activity have been evaluated. The addition of isolated TGase to fish mince from Cynoglossus sp. was attempted in order to evaluate the setting and gelling ability. The setting and gelling ability of fish mince in presence of TGase improved considerably as revealed by small strain and large strain test.     

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.     

High Pressure Effects on Gelation of Surimi and Turkey Breast Muscle Enhanced by Microbial Transglutaminase

High pressure effects on the strength (stress) and elasticity/deformability (strain) of surimi and turkey breast meat gels containing microbial transglutaminase (TGase) were evaluated. Pressurization of muscle proteins at 4°C prior to incubation at 25°C or 40°C (setting) increased gel strength 2–3 fold in uncooked surimi gels, but not in uncooked turkey gels. However, pressurization at 40°C or 50°C prior to setting increased the strength of turkey gels. Similar effects of prior pressurization, but of lesser magnitude, occurred in gels formed by directly or subsequently (following setting) cooking at 90°C. SDS-PAGE confirmed that myosin crosslinking occurred due to TGase activity during the setting treatment, which had survived prior pressure treatment. High pressure rendered protein substrates more accessible to TGase thereby enhancing intermolecular cross-link formation and gel strength.     

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 iced storage of bigeye snapper (Priacanthus tayenus) on the chemical composition,properties and acceptability of Som-fug,a fermented Thai fish mince

The effect of iced storage of bigeye snapper (Priacanthus tayenus) on the chemical composition, properties and acceptability of Som-fug was investigated. During 15 days of iced storage, total volatile base (TVB), trimethylamine (TMA) and TCA-soluble peptide contents as well as thiobarbituric reactive substances (TBARS) of fish muscle increased continuously after 3 days of storage (p < 0.05). It was suggested that deterioration, protein degradation and lipid oxidation proceeded with increasing storage time. Som-fug prepared from surimi of bigeye snapper stored in ice for different times had similar pH, acidity and lactic acid bacteria count at the end of the fermentation (30 °C, 48 h). Generally, higher content of TCA-soluble peptides and higher TBARS were found in fermented Som-fug produced from bigeye snapper stored in ice for a longer time (p < 0.05). Hardness, adhesiveness, springiness, cohesiveness, and resilience of fermented Som-fug decreased with a concomitant increase in weight loss, released water and expressible water contents when fish kept for a longer time were used (p < 0.05). L^∗, a^∗, b^∗, whiteness and the likeness for appearance, colour, texture and flavour of Som-fug decreased when fish kept in ice for an extended time were used (p < 0.05). However, the taste likeness was not affected by iced storage time (p > 0.05). No differences in overall liking were noticeable when fish kept in ice for up to 12 days were used for Som-fug production (p > 0.05). Therefore, the quality of fish used as raw material should be an important factor in determining the characteristics of Som-fug.     

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