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Antioxidative activities of phenolic compounds (caffeic acid, gallic acid and tannic acid; 200 ppm) in washed mince (pH 6), with added myoglobin (Mb) and haemoglobin (Hb), from bighead carp (Hypophthalmichthys nobilis), during 9 days of iced storage, were studied. Tannic acid exhibited the preventive effect on discolouration of washed mince containing Mb or Hb during storage (P<0.05). High peroxide value (PV) was found and large amount of, thiobarbituric acid-reactive substances (TBARS) and hexanal were formed in washed mince containing haem proteins, especially Hb. As determined by apo Streptococcal haem-associated protein, Hb had the lower haem affinity than Mb. Phenolic compounds, especially caffeic acid and gallic acid, could lower lipid oxidation induced by Mb or Hb throughout storage (P<0.05). Prevention of haem release, as well as inhibition of lipid oxidation induced by haem proteins with selected phenolic compounds, should be an alternative means in lowering discolouration and lipid oxidation in fish muscle., (Copyright © 2012 Elsevier Ltd. All rights reserved.)

Background: Oxidation of myoglobin is responsible for the undesirable appearance and loss in acceptability of fish and fish products. The retardation of such a change by a modification of the surrounding atmosphere would be a means to maintain the quality of fish during the refrigerated storage., Results: The changes in oxymyoglobin and metmyoglobin from dark muscle of Eastern little tuna (Euthynnus affinis) as affected by different atmospheric systems (closed system, opened system and flushed oxygen system) were determined. A saturated oxygen atmosphere more likely weakened the haem-globin complex, especially as the exposure time increased. Autoxidation of the oxy form proceeded rapidly in the presence of oxygen with the concomitant formation of the met form. When the oxygen was excluded, oxidation of oxymyoglobin was retarded. With flushed oxygen and increasing exposure time, conformational changes of globin occurred, mainly associated with protein oxidation. Generally, oxymyoglobin was more susceptible to oxidation and conformational change than did metmyoglobin. After keeping the samples at 4 °C for 3 days, dark muscle of tuna fillet kept in vacuum packaging had a slight decrease in redness and it was still acceptable. The fillets stored in exposed air or packed in 100% O(2) atmosphere turned brown, most likely due to myoglobin oxidation., Conclusion: The oxygen level of the packaging atmosphere had a profound impact on myoglobin alteration, which was governed by the forms of myoglobin., (Copyright © 2011 Society of Chemical Industry.)

Unlabelled: The effect of pH (6.0, 6.5, and 7.0) on lipid oxidation in washed Asian seabass (Lates calcarifer) mince mediated by oxymyoglobin from the dark muscle of little Eastern tuna (Euthynnus affinis) during 8 d of refrigerated storage was studied. Metmyoglobin formation and discoloration increased with increasing storage time and the changes were more pronounced at lower pH. The highest lipid oxidation and off-odor development were observed when myoglobin was incorporated in washed mince at pH 6.0. At low pH, oxidation of myoglobin took place and lipid oxidation in washed mince was enhanced. This was concomitant with the increased fishy and rancid off odor in the sample containing myoglobin, especially at pH 6.0. Washed mince containing myoglobin at pH 6.0 had 1-octen-3-ol and hexanal as the major volatile compounds. Thus, postmortem pH and myoglobin played an essential role in lipid oxidation and off odor in fish muscle during the extended storage., Practical Application: Myoglobin plays a role in the color of fish muscle. The change of myoglobin affects not only consumer acceptability, but also lipid oxidation as well as odor. The control of pH of muscle could be a potential means to lower the lipid oxidation mediated by myoglobin. As a consequence, the prime quality of fish with a negligible fishy odor could be maintained during postharvest handling or storage.

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 beta-chain but a lower content of alpha-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 degrees 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 (c) 2009 Society of Chemical Industry.)