The purpose of this study was to determine the effect of pre-rigor salting on the quality characteristics of surimi gels prepared from snakehead fish muscle. Pre-rigor and post-rigor muscle were mixed with 0.3% or 3% NaCl (w/w) and made into surimi gels, respectively. Results showed that pre-rigor muscle had a higher content of ATP, longer sarcomere, higher pH and greater protein solubility. Metabolic profile suggested that pre-rigor muscle had higher content (a 28-fold increase) of antioxidants such as butyryl-l-carnitine. Transmission electron microscopy showed more damage of mitochondria in post-rigor muscle. Surimi paste from pre-rigor meat chopped with 3% NaCl generally showed greater radical scavenging ability and had higher content of free sulfhydryl. Surimi gel made from pre-rigor muscle salted with 3% NaCl showed a larger gel strength (3.18 kg*mm vs. 2.22 kg*mm) and better water-holding (86% vs. 80%) than that of post-rigor group. Based on these findings, we hypothesized that: In addition to other factors such as pH, degree of denaturation, etc., less protein oxidation in pre-rigor salted surimi also contributes to the improved gel properties.

In order to clarify the individual role of freezing and frozen storage on the quality of fish, fillets of large-mouth bass (Micropterus salmoides) were subjected to different freezing rates (freezing with -18 °C (A), -60 °C (B), and -60 °C with forced air circulation at 2 m/s (C), respectively) followed by frozen storage at -18 °C for 30 and 90 days. Another two groups were frozen at -60 °C, followed by storage at -40 °C (D) and -60 °C (E), respectively. Results showed that water-holding and TVBN were mainly affected by storage time. No significant changes were found in free thiol content among treatments. A greater freezing rate and lower storage temperature generally led to lower TBARS. GC × GC-TOFMS revealed a total of 66 volatile compounds, which were related to lipid oxidation. PLS-DA showed that fresh samples were separated from the frozen-thawed ones, and fillets in groups D and E were relatively close to fresh fillets in the composition of oxidation-related volatiles. In conclusion, freezing rate and storage temperature had a significant impact on lipid oxidation and protein denaturation in the fillets of large-mouth bass, while protein oxidation was more affected by freezing rate.

The structural inconsistencies in commercial algal alginates have limited their reliability and quality for various applications. Therefore, the biosynthesis of structurally consistent alginates is crucial to replace the algal alginates. Thus, this study aimed to investigate the structural and alginate\'s structural and functional properties of Pseudomonas aeruginosa CMG1418 as a substitute. To achieve this, the CMG1418 alginates were physiochemically characterized using various techniques such as transmission electron microscopy, Fourier-transform infrared 1H-NMR, 13C-NMR, and gel permeation chromatography. The synthesized CMG1418 alginate was then subjected to standard tests to evaluate its biocompatibility, emulsification, hydrophilic, flocculation, gelling, and rheological properties. The analytical studies revealed that CMG1418 alginate is an extracellular and polydisperse polymer with a molecular weight range of 20 000-250 000 Da. It comprises 76% poly-(1-4)-β-D-mannuronic acid (M-blocks), no poly-α-L-guluronate (G-blocks), 12% alternating sequences of β-D-mannuronic acid and α-L-guluronic acid (poly-MG/GM-blocks), 12% MGM-blocks, 172 degrees of polymerization, and di-O-acetylation of M-residues. Interestingly, CMG1418 alginate did not show any cytotoxic or antimetabolic activity. Moreover, compared to algal alginates, CMG1418 alginate exhibited higher and more stable flocculation efficiencies (70-90%) and viscosities (4500-4760 cP) over a wide range of pH and temperatures. Additionally, it displayed soft to flexible gelling abilities and higher water-holding capacities (375%). It also showed thermodynamically more stable emulsifying activities (99-100%) that surpassed the algal alginates and commercial emulsifying agents. However, only divalent and multivalent cations could slightly increase viscosity, gelling, and flocculation. In conclusion, this study explored a structurally di-O-acetylated and poly-G-blocks-deficient, biocompatible alginate, and its pH and thermostable functional properties. This research suggests that CMG1418 alginate is a superior and more reliable substitute for algal alginates in various applications, such as viscosifying, soft gelling, flocculating, emulsifying, and water-holding.

Marine microbes produce polysaccharides with unique physicochemical and functional properties that help them survive in harsh marine environments. However, only a handful of marine exopolysaccharides (EPSs) have been reported to date. The present study explored the seashore of Visakhapatnam, India, to report a novel exopolysaccharide designated as Br42 produced by Brevibacillus borstelensis M42. The isolate was identified through morphological, biochemical, phylogenetic, and genome sequencing analysis. The studies on fermentation kinetics revealed that EPS Br42 was a primary metabolite with a maximum production of 1.88 ± 0.02 g/L after 60 h when production broth was fortified with 2% glucose. Additionally, EPS Br42 was found to be a heteropolysaccharide consisting of glucose and galacturonic acid with a molecular weight of about 286 kDa. Interestingly, this molecule possesses industrially relevant functional properties such as water-holding (510 ± 0.35%), oil-holding (374 ± 0.12% for coconut oil and 384 ± 0.35% for olive oil), and swelling capacities (146.6 ± 5.75%). EPS Br42 could form an emulsion that was stable at a wide pH range for about 72 h and, in fact, performed better as compared to Span 20, a commercially used synthetic emulsifier. Moreover, this EPS was also found to be heat stable and exhibited non-Newtonian pseudoplastic behavior. These physicochemical and functional properties of polysaccharides suggest that the EPS Br42 has potential for multifarious industrial applications as an emulsifier, stabilizer, viscosifier, and binding agent.

This study aimed to determine the effects of multiple freeze-thaw (FT) cycles (0, 1, 2, and 4) on the physicochemical properties, water-holding status, and nutritional values of broiler drumsticks. The results showed that L* (lightness) and b* (yellowness) values, thiobarbituric acid-reactive substances, total volatile basic nitrogen, and total viable counts significantly increased but pH values, protein solubility, and sensorial acceptance decreased after four FT cycles (P ˂ 0.05). The decreases in moisture content thawing loss, centrifugation loss, drip loss, and cooking loss indicated that the water-holding capacities of samples subjected to multiple FT cycles were diminished. Results of cell microstructure analysis and sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed the occurrence of ruptured muscle cells with decreased fiber diameters and changes in myosin heavy chain band intensity after multiple FT cycles (P ˂ 0.05). As the number of FT cycles increased, the content of total free amino acids and polyunsaturated fatty acids including linoleic (C18:2), linolenic (C18:3), eicosatetraenoic (EPA, C20:5), and docosahexaenoic (DHA, C22:6) acids decreased (P ˂ 0.05). In conclusion, four repeated FT cycles accelerated the deterioration of physiochemical properties, reduced the water-holding status, and considerably impaired sensory characteristics and nutritional values of chicken meat.

The basic contractile unit of muscle, the sarcomere, will contract as the muscle goes into rigor post-mortem. Depending on the conditions, such as the rate of pH decline, the cooling rate and the mechanical restraints on the muscles, this longitudinal shortening will result in various post-mortem sarcomere lengths as well as lateral differences in the distances between the myosin and actin filaments. This shortening is underlying the phenomena described as rigor contraction, thaw rigor, cold shortening and heat shortening. The shortening in combination with the molecular architecture of the sarcomere as defined by the myosin filaments and their S-1 and S-2 units, the interaction with the actin filaments, and the boundaries formed by the Z-disks will subsequently influence basic meat quality traits including tenderness and water-holding capacity. Biochemical reactions from proteolysis and glycogen metabolism interrelate with the sarcomere length in a complex manner. The sarcomere length is also influencing the eating quality of cooked meat and the water-holding in meat products.