The impact of desmin on texture and water‐holding capacity of ice‐stored grass carp (Ctenopharyngodon idella) fillet

The objective of this work was to analyse the role of desmin in texture softening and water‐holding capacity (WHC) of ice‐stored grass carp fillet. Results indicated that shear force of the fillet decreased sharply within 3 days, while drip loss increased during the whole ice storage. Water mobility and distribution were measured by low‐field ¹H NMR T₂ relaxation that revealed a positive correlation (P < 0.01) between WHC and the mobility of the immobilised water (T₂₁ relaxation time). Meanwhile, negative correlation could be established between intact desmin and drip loss (P < 0.01). Intact desmin was extremely correlated with shear force (P < 0.01) and positively correlated with calpains activity (P < 0.05). This study demonstrated that the degradation of desmin was involved in the mobility of the myofibrillar water and softening of grass carp fillet during ice storage. Furthermore, calpains autolysis seemed to result in desmin degradation.     

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

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

Superchilled,chilled and frozen storage of Atlantic mackerel (Scomber scombrus) fillets – changes in texture,drip loss,protein solubility and oxidation

Changes in quality characteristics in relation to protease activity and protein oxidation in chilled, superchilled and frozen mackerel fillets during storage were studied. The solubility of sarcoplasmic proteins was quite stable in mackerel samples for all storage experiments, whereas the solubility of myofibrillar proteins decreased in both superchilled and frozen samples. A significant correlation (r = 0.983, P < 0.05) between the increased activity of cathepsin B+L in chilled fillets and softening of the fish flesh during storage was revealed. Contrary with chilled samples, the texture of superchilled mackerel fillets became tougher along the storage period, which can be explained by a higher rate of myofibrillar oxidation (r = 0.940, P < 0.05). The hardness and drip loss decreased slightly at the end of frozen storage. Superchilling preserved the quality of mackerel fillets with the least side effects in relation to protein solubility, drip loss and softening of the fish tissue as compared to chilled and frozen storage.     

Effect of total milk solid content adjusted by adding ultrafiltered milk retentate on quality of set mango yoghurt

The quality of set mango yoghurt prepared by varying total milk solids (TMS) level in mango yoghurt mix, by adding 5× ultrafiltered cow skim milk retentate and cow milk cream, was investigated. The water‐holding capacity (WHC) and values of textural attributes of mango yoghurt increased, whereas body and texture and overall acceptability scores decreased significantly (P < 0.05) with increasing TMS level. The optimised product (10.2% TMS level) was compared with conventional mango yoghurt. Acetaldehyde concentration, WHC, values of textural attributes, body and texture, overall acceptability scores and pH were significantly (P < 0.05) higher in optimised compared with conventional mango yoghurt.     

Acid‐soluble and pepsin‐soluble collagens from grass carp (Ctenopharyngodon idella) skin: a comparative study on physicochemical properties

In this study, acid‐soluble (ASC) and pepsin‐soluble (PSC) collagens with triple helical structures were successfully extracted from the skin of grass carp (Ctenopharyngodon idella) by two different extraction approaches. SDS‐PAGE pattern revealed that ASC and PSC are type I collagens with typical α1, α2 and β‐chains. In addition, the intensity of χ‐chain (trimer) in ASC was higher than that of PSC, representing the presence of the high proportion of intra‐ and intermolecular cross‐links of extracted collagens with large molecular weight using the acid method. Differential scanning calorimetry (DSC) results demonstrate that T_d (69.04 °C) of ASC was higher than T_d (62.20 °C) of PSC. Both ASC and PSC had the highest solubility at acidic pHs or at a low concentration of NaCl (<2%, w/v). The results of FTIR suggested the ASC and PSC maintained in the helical secondary structure at high degree.     

The impact of crucial protein degradation in intramuscular connective tissue on softening of ice-stored grass carp (Ctenopharyngodon idella) fillets

This study aimed to determine the role of intramuscular connective tissue (IMCT) in softening of ice-stored grass carp (Ctenopharyngodon idella) fillet. The change in important proteins in IMCT and impact of IMCT destruction in fish softening were both investigated. The exogenous collagenase was used to differentiate the role of IMCT. Results showed that decorin, elastin and collagen in IMCT decreased by 71%, 48% and 54%, respectively. Decorin and elastin were mainly degraded in the primary stage, while collagen decreased mainly in the later stage. Then, IMCT destruction experiment showed that collagenase was quite effective for destruction of IMCT, while myofibre tissue was not affected. Subsequently, specific role of IMCT could be distinguished. Decrease in shear force became twofold faster in the collagenase group at the beginning than that in the control group, indicating a quite important role of IMCT in maintaining fish texture, especially in the primary stage of storage.     

Effect of lightly salt and sucrose on rigor mortis changes in silver carp (Hypophthalmichthys molitrix) stored at 4°C

To evaluate the effect of salt and sucrose on rigor mortis changes in silver carp during 72 h at 4 °C, physical (texture parameters, water holding capacity (WHC), cooking loss, L* value) and chemical adenosine triphosphate (ATP‐related compounds, K value, pH value) characteristics were studied. Silver carp were subjected to following treatments: left untreated (CK), treated with 1.8% salt (S) and 1.8% salt incorporating 1.8% sucrose (S+S). Curing treatments predominantly increased IMP content, WHC and texture parameters, retarded cooking loss and discoloration compared with untreated samples. The highest IMP concentration measured in S and S+S all occurred at 4 h, which was prior to that of CK (48 h). K value of S+S did not follow a linear relationship with time. The results indicated that the best eating times of CK, S and S+S were 2, 4 and 4 h at 4 °C, respectively, and curing treatments improved the quality of silver carp during postmortem process.     

草鱼皮酸溶性和酶溶性胶原蛋白的提取及性质

本文研究了从草鱼皮中提取酸溶性胶原蛋白(ASC)和酶溶性胶原蛋白(PSC)及其部分性质。草鱼皮中ASC和PSC的提取得率以干基计分别为8.0%和18.6%;对草鱼皮ASC和PSC的紫外光谱分析,最大吸收峰都接近223nm;SDS-PAGE电泳图谱显示草鱼皮胶原蛋白是由两条不同的α链组成,分子量都在100kDa以上,与猪皮I型胶原蛋白相似;草鱼皮ASC和PSC热变性温度分别为33.8、34.5℃,只比猪皮的热变性温度(37℃)低3℃左右。结果表明草鱼皮胶原蛋白在功能食品、医药、化妆品、制药等方面有潜在的应用。     

Inhibition of frozen storage‐induced oxidation and structural changes in myofibril of common carp (Cyprinus carpio) surimi by cryoprotectant and hydrolysed whey protein addition

The objective of the present study was to evaluate the efficacy of combined cryoprotectants (sucrose + sorbitol) and whey protein isolate (WPI) hydrolysates to inhibit protein oxidation and quality loss in common carp (Cyprinus carpio) surimi during frozen storage at ?25 °C. With increasing storage time, the carbonyl content of myofibrillar proteins increased from 4.02 nmolmg^‐1 protein (0 day) to 7.25, 6.31, 5.26 and 4.83 nmol mg^?1 protein (180 days; P < 0.05) for the control and samples with cryoprotectants, with cryoprotectants + WPI hydrolysates and with cryoprotectants + propyl gallate, respectively; protein surface hydrophobicity and turbidity increased in a similar trend, while sulfhydryl content, Ca‐ATPase activity, protein solubility and protein thermal stability decreased (P < 0.05). These results suggest that treatments with combined cryoprotectants and antioxidative WPI hydrolysates offer an effective approach to reducing the extent of protein oxidation in common carp surimi, thereby limiting protein structural changes known to impair texture of surimi products.     

The function of endogenous cathepsin in quality deterioration of grass carp (Ctenopharyngodon idella) fillets stored in chilling conditions

Changes of textural properties and cathepsin activity of grass carp fillets during storage in superchilling (?1.5 ± 0.2 °C) and ice (0.2 ± 0.1 °C) was investigated, and the function of cathepsin in quality deterioration of grass carp fillets was discussed. Results showed that shear force of superchilled and ice‐stored fillets decreased by 50% and 55% after 6 days of storage, respectively. The cathepsin activies in different fractions changed significantly during storage at both conditions. Cathepsin B, B+L activities in sarcoplasma, myofibrillar and heavy mitochondrial fraction significantly increased during the early 3 days postmortem, accompanied by remarkable reduction of corresponding activity in lysosome. Cathepsin D activity in sarcoplasma and myofibrillar significantly increased during 6 days of storage with corresponding decrease in lysosome and heavy mitochondria. Correlation analysis showed that changes of shear force of grass carp fillets were significantly correlated with integration of cathepsin B, D and B+L throughout storage time (r² > 0.94). As derived from the first‐order exponential decay model, the enzyme efficiencies (k_a) of cathepsin B and B+L were more than twofold higher than those of cathepsin D, suggesting the major role of cathepsin B and B+L in textural deterioration of grass carp fillets in chilling storage.     

Broad‐spectrum inhibition of proteolytic enzymes by allicin and application in mitigating textural deterioration of ice‐stored grass carp (Ctenopharyngodon idella) fillets

The inhibitory effect of allicin on proteolytic enzymes and textural deterioration of ice‐stored grass carp (Ctenopharyngodon idella) fillets was investigated. The results of in vitro study showed that allicin inhibited the activity of cathepsin B, L and D, calpain and collagenase in crude extract of grass carp muscle. Among endogenous enzymes, cathepsin B, L and collagenase were the most susceptible to allicin. Proteolysis of myofibrillar proteins by either crude enzyme or cathepsin B and L was almost prevented by allicin when employed at a concentration higher than 100 mm . After storage of 21 days, shear force of fillets treated with allicin at 10–100 mm was 39–51% higher than that of control. Myofibrillar proteins of fillets during storage were well protected against degradation when allicin concentration increased to 100 mm , as evidenced by SDS‐PAGE. Therefore, allicin could be a potential broad‐spectrum inhibitor to retard softening of fish fillets via mitigating myofibrillar proteolysis by endogenous enzymes especially cathepsin B and L during ice‐storage.     

冷藏过程中草鱼肌肉蛋白质特性的变化

将草鱼在4℃条件冷藏0、2、4、6、8、10 d后,提取并制备其肌肉蛋白质样品,以体积排阻色谱、流变仪、差示扫描量热法等方法分析其蛋白质分子量分布、持水性能、溶液黏度、热力学性质及肌动球蛋白盐溶性的变化。结果显示,随着冷藏时间的延长,草鱼肌肉蛋白质分子量总体变小,持水力、溶液黏度、肌动球蛋白溶出量均呈下降趋势,热变性焓先降低后升高;其中持水力冷藏前期下降剧烈,第8 d降幅达56.12%;黏度在低剪切速率下下降明显,在剪切速率20 s^-1条件下黏度由第0 d的0.89 Pa·s降至第10 d的0.05 Pa·s;肌动球蛋白的溶出量在冷藏前6 d下降趋势明显,冷藏第6 d时降幅达40.96%;冷藏后的蛋白质样品的DSC曲线出现两个吸热峰,其最大峰的起始温度和峰顶温度均在第6 d时最大,而热变性焓在第6 d时最低,表明冷藏第6 d是草鱼肌肉蛋白质变化的关键时间点。研究结果为了解冷藏过程中草鱼肌肉品质劣变机制提供了基础数据。     

Characterisation of acid-soluble collagen from skin of silver carp (Hypophthalmichthys molitrix)

Acid-soluble collagen (ASC) from the skin of silver carp (Hypophthalmichthys molitrix) was isolated and some properties of ASC were investigated. SDS–PAGE patterns showed ASC from silver carp skin was type ? collagen. Sulfopropyl-Toyopearl 650(M) column chromatography indicated that ASC from silver carp skin was composed of three kinds of α chains, α₁, α₂ and α₃. Hydroxyproline and proline content of ASC from silver carp skin was 192 residues/1000 residues, which was similar to that of ASC from carp skin. Denaturation temperature (T_d) of ASC from silver carp skin was around 29 °C. The results showed that some properties of ASC from silver carp skin were similar to those of ASC from carp skin. However, the peptide map of ASC from silver carp skin digested by pepsin was distinguished with that of ASC from carp skin.     

Grass carp peptides hydrolysed by the combination of Alcalase and Neutrase: Angiotensin‐I converting enzyme (ACE) inhibitory activity,antioxidant activities and physicochemical profiles

In this study, grass carp peptides were prepared by enzymatic hydrolysis of grass carp protein using the combination of Alcalase and Neutrase, and angiotensin‐I converting enzyme (ACE) inhibitory activity in vitro, antihypertensive activity in vivo, antioxidant activities, and physicochemical properties of peptides achieved from grass carp protein were characterised after ultrafiltration and desalted processes using mixed ion exchange resins. The purified peptides exhibited strong ACE inhibitory activity (IC₅₀ = 105 μg mL^?1), antihypertensive activity with the maximal drop for systolic blood pressure (SBP) of 43 mmHg at a dosage of 100 mg per kg body weight in spontaneously hypertensive rat (SHR), and antioxidant activities indicated by thiobarbituric acid‐reactive substance values in a liposome‐oxidising system, radical‐scavenging activity and chelation of metal ions (Fe²⁺). The molecular weight of peptides was <1000 Da. Compared to grass carp protein, the peptides separated from enzymatic hydrolysates possessed similar amino acid compositions, but contained higher concentrations of essential amino acids. Moreover, the peptides exhibited excellent solubility at a wide range of pH values from 2 to 10, and lower apparent viscosity than the protein. The peptides separated from enzymatic hydrolysates might be used as a promising ingredient in antihypertensive functional foods and nutraceuticals.     

Compositional and physicochemical characteristics of acid solubilized collagen extracted from the skin of unicorn leatherjacket (Aluterus monoceros)

Acid solubilized collagen (ASC) was extracted from the skin of unicorn leatherjacket (Aluterus monoceros) using 0.5 M acetic acid, followed by precipitation with 2.6 M NaCl. ASC with the yield of 4.19% (wet weight basis) was identified as type I collagen, which was composed of two α₁ chains and one α₂ chain. Different peptide maps were observed between ASC hydrolyzed by V8 protease and lysyl endopeptidase. The maps were also different from those of type I collagen from calf skin, suggesting the differences in amino acid sequences between both collagens. Glycine was the most predominant amino acid. ASC contained the relatively higher content of alanine, but lower contents of proline and hydroxyproline, compared with calf skin collagen. FTIR analysis showed that ASC was in triple helix structure. T_max of ASC dispersed in 0.05 M acetic acid and deionized water were 27.7 and 35.8 °C, respectively. Relative viscosity of 0.03% (w/v) ASC dissolved in 0.1 M acetic acid decreased continuously as the temperature increased from 4 to 52 °C, indicating thermal destabilization or denaturation of ASC molecules. ASC had the solubility greater than 90% in very acidic pH range (pH 1–4) and the solubility decreased continuously with increasing NaCl concentrations (0–6%). Net charge of ASC and calf skin collagen became zero at pHs of 5.58 and 5.68, respectively as determined by zeta potential titration. Therefore, skin of unicorn leatherjacket can be used as an alternative collagenous source.     

Effect of salt content on gelation of normal and wooden breast myopathy chicken pectoralis major meat batters

This study investigated the effects of salt content (0–4%) on water holding capacity (WHC), textural characteristics, rheological properties, and microstructure of cooked normal (NOR) and wooden breast (WB) chicken meat batters. Results indicated with 0–2% salt addition, the WB batters had significantly lower WHC and storage modulus (G’) compared with the NORs (P < 0.05). However, these differences were eliminated when salt contents were increased to 3% or 4%. In addition, the NORs formed more regular and pored networks than the WBs (0–2%). Salt level significantly affected the textural properties of both batter types (P < 0.05). The hardness of the WB batters was lower than NORs at all NaCl levels (P < 0.05). Overall, compared with NORs, the WB batters showed inferior gelation properties at salt contents of 0–2%, while increasing salt content to 3–4% can improve the WHC and microstructure of gels.     

Effect of previous frozen storage on quality changes of grass carp (Ctenopharyngodon idellus) fillets during short‐term chilled storage

The effect of chilled, frozen and freeze‐chilled storage on quality of grass carp fillets and soups was evaluated by sensory score, total aerobic counts and biochemical quality. Fish fillets were stored at 4 °C for 6 days (T1), ?40 °C for 12 h and then at ?20 °C for 5 days (T2), ?40 °C for 12 h and then at ?20 °C for 5 days, followed by at 4 °C for 4 days (T3). T1 showed higher sensory score, salt‐soluble protein content, better colour and texture qualities than T2 and T3 within 3 days. All fillets kept good quality based on the acceptable limit of sensory score, total volatile basic nitrogen and total aerobic count during storage time. According to the transportation and retail time, chilled storage is appropriate when it is within 3 days. If it extends for 5 days, freeze‐chilling treatment keeps better quality, but later chilled fillets should be retailed within 4 days.     

Production of high quality gels from sea bass: Effect of MTGase and dietary fibre

The effects of MTGase (5 g/kg, w/w) and dietary fibre (inner pea fibre, 40 g/kg, w/w, carrageenan, 10 g/kg, w/w, carrageenan + konjac flour, 10 + 10 g/kg, w/w) on heat-induced gels from sea bass (Dicentrarchus labrax) trimmings were studied. MTGase incorporation had a positive effect on texture: gel strength and force at rupture increased. MTGase reduced protein solubility, meaning greater protein aggregation, according to electropherograms. Pea fibre had no positive effects: texture was quite similar to that of the control products and WHC was reduced. Carrageenan addition had no deleterious effect upon the texture of the gels and made them harder and springier. Force at rupture (even without MTGase) and WHC were greatly improved. Combination of carrageenan and konjac further enhanced these effects. For those gels without MTGase, protein solubility in urea and urea + DTT was reduced by both fibres, suggesting a reduction of hydrogen bonding between proteins.     

Collagen changes in refrigerated sea bass muscle treated with pyrophosphate and stored in modified- atmosphere packaging

Changes in collagen of sea bass muscle treated with and without pyrophosphate (PP) were monitored during storage in modified-atmosphere packaging (MAP) (80% CO₂, 10% O₂ and 10% N₂) at 4 °C. No changes in acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) of sea bass muscle with and without PP treatment were observed during storage in MAP up to 21 days. However, a slight decrease in insoluble collagen (ISC) of a sample kept in MAP was found. For sea bass muscle stored under an air atmosphere ASC increased, whereas PSC and ISC decreased with a concomitant loss in the firmness     

The effect of linseed and psyllium fibre on the gelling properties of unwashed mince from farmed meagre (Argyrosomus regius)

The gelling properties of farmed meagre (Argyrosomus regius) mince mixed with linseed and/or psyllium fibres (up to 4.0%, w/w) were studied. The effects of chilled storage time (15 days vs. 1 day) and cold gelling (setting at 2 ± 2 °C) were measured. Linseed addition increased ω3 PUFA content and worsened the gel products' texture. Psyllium functional fibre addition had only a negative effect upon breaking force and deformation, not affecting the remaining textural properties and improving water‐holding capacity (WHC) from 61–77 to 70–85%. The incorporation of 4.0% (w/w) psyllium seems to be advisable. Quality of heat‐induced meagre gels was unaffected by chilled storage time. Production of an acceptable cold set gel is feasible provided that enough time is allowed for completion of the setting process. Overall results showed a potential for combining small‐sized meagre (<2 kg) and psyllium fibres to produce high added‐value functional foods.