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Pathway-oriented action of dietary essential oils to prevent muscle protein oxidation and texture deterioration of farmed rainbow trout

Santos, H.M.C., Méndez, L., Secci, G., Parisi, G., Martelli, R., Medina, I.·2019·Animal
DOI 10.1017/s1751731119000016
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Figure 1 Effect of diet and frozen storage on carbonylation level of sarcoplasmic and myo fi brillar proteins from rainbow trout (Oncorhynchus mykiss) muscle. (a) Representative mono-dimensional electrophoresis (1-DE) fl uorescein-5-thiosemicarbazide (FTSC)-stained gel of sarcoplasmic proteins from control diet during 165 days of frozen storage ( -10°C). (b) Representative 1-DE FTSC-stained gel of sarcoplasmic proteins from essential oil diet during 165 days of frozen storage ( -10°C). (c) Representative 1-DE FTSC-stained gel of myo fi brillar proteins from control diet during 165 days of frozen storage ( -10°C). (d) Representative 1-DE FTSC-stained gel of myo fi brillar proteins from essential oil diet during 165 days of frozen storage ( -10°C).
Figure 1 Effect of diet and frozen storage on carbonylation level of sarcoplasmic and myo fi brillar proteins from rainbow trout (Oncorhynchus mykiss) muscle. (a) Representative mono-dimensional electrophoresis (1-DE) fl uorescein-5-thiosemicarbazide (FTSC)-stained gel of sarcoplasmic proteins from control diet during 165 days of frozen storage ( -10°C). (b) Representative 1-DE FTSC-stained gel of sarcoplasmic proteins from essential oil diet during 165 days of frozen storage ( -10°C). (c) Representative 1-DE FTSC-stained gel of myo fi brillar proteins from control diet during 165 days of frozen storage ( -10°C). (d) Representative 1-DE FTSC-stained gel of myo fi brillar proteins from essential oil diet during 165 days of frozen storage ( -10°C).CC-BY-NC-ND · From the PDF
Figure 2 Individual carbonylation indices of sarcoplasmic (a) and myo fi brillar (b) proteins corresponding to 75 and 165 days of frozen storage ( -10°C) in muscle of rainbow trout (Oncorhynchus mykiss) from control (C) and essential oil (M) diets. The values are expressed as fold change regarding to initial time (0 days). PYGM = glycogen phosphorylase muscle form; PKM = pyruvate kinase isozymes M1/M2; CKM = creatine kinase M-type; ALDOA = fructose bisphosphate aldolase A; G3PDH = glyceraldehyde-3-phosphate dehydrogenase; PGM2 = phosphoglycerate mutase 2; TPI = triosephosphate isomerase; MHC = myosin heavy chain fast skeletal muscle; PFKM = 6-phosphofructokinase muscle type. *Represents signi fi cant differences (P < 0.05) between diets.
Figure 2 Individual carbonylation indices of sarcoplasmic (a) and myo fi brillar (b) proteins corresponding to 75 and 165 days of frozen storage ( -10°C) in muscle of rainbow trout (Oncorhynchus mykiss) from control (C) and essential oil (M) diets. The values are expressed as fold change regarding to initial time (0 days). PYGM = glycogen phosphorylase muscle form; PKM = pyruvate kinase isozymes M1/M2; CKM = creatine kinase M-type; ALDOA = fructose bisphosphate aldolase A; G3PDH = glyceraldehyde-3-phosphate dehydrogenase; PGM2 = phosphoglycerate mutase 2; TPI = triosephosphate isomerase; MHC = myosin heavy chain fast skeletal muscle; PFKM = 6-phosphofructokinase muscle type. *Represents signi fi cant differences (P < 0.05) between diets.CC-BY-NC-ND · From the PDF
Figure 3 Evolution of individual carbonylation indices corresponding to the myo fi brillar (a) α -actinins-1, (b) -3 and (c) actin from 75 to 165 days of frozen storage ( -10°C) in muscle of rainbow trout (Oncorhynchus mykiss) from control (C) and essential oil (M) diets. Evolution in protein amount of (d) actin is also showed for this experimental period. All values are expressed as fold change regarding to the initial time (0 days). *Represents signi fi cant differences (P < 0.05) between diets.
Figure 3 Evolution of individual carbonylation indices corresponding to the myo fi brillar (a) α -actinins-1, (b) -3 and (c) actin from 75 to 165 days of frozen storage ( -10°C) in muscle of rainbow trout (Oncorhynchus mykiss) from control (C) and essential oil (M) diets. Evolution in protein amount of (d) actin is also showed for this experimental period. All values are expressed as fold change regarding to the initial time (0 days). *Represents signi fi cant differences (P < 0.05) between diets.CC-BY-NC-ND · From the PDF
Figure 4 Effect of diet and frozen storage on total protein level of sarcoplasmic and myo fi brillar proteins from rainbow trout (Oncorhynchus mykiss) muscle. (a) Representative mono-dimensional electrophoresis (1-DE) Coomassie blue-stained gel of sarcoplasmic proteins from control diet during 165 days of frozen storage ( -10°C). (b) Representative 1-DE Coomassie blue-stained gel of sarcoplasmic proteins from essential oil diet during 165 days of frozen storage ( -10°C). (c) Representative 1-DE Coomassie blue-stained gel of myo fi brillar proteins from control diet during 165 days of frozen storage ( -10°C). (d) Representative 1-DE Coomassie blue-stained gel of myo fi brillar proteins from essential oil diet during 165 days of frozen storage ( -10°C).
Figure 4 Effect of diet and frozen storage on total protein level of sarcoplasmic and myo fi brillar proteins from rainbow trout (Oncorhynchus mykiss) muscle. (a) Representative mono-dimensional electrophoresis (1-DE) Coomassie blue-stained gel of sarcoplasmic proteins from control diet during 165 days of frozen storage ( -10°C). (b) Representative 1-DE Coomassie blue-stained gel of sarcoplasmic proteins from essential oil diet during 165 days of frozen storage ( -10°C). (c) Representative 1-DE Coomassie blue-stained gel of myo fi brillar proteins from control diet during 165 days of frozen storage ( -10°C). (d) Representative 1-DE Coomassie blue-stained gel of myo fi brillar proteins from essential oil diet during 165 days of frozen storage ( -10°C).CC-BY-NC-ND · From the PDF
Figure 5 Evolution of protein solubility and global carbonylation in sarcoplasmic (a) and myo fi brillar (b) protein fractions during 165 days of frozen storage ( -10°C) in muscle of rainbow trout (Oncorhynchus mykiss) fed control (C) and essential oil (M) diets. The values corresponding to each time are expressed as fold change regarding to initial time (0 days). Means with different lowercase letters are signi fi cantly different at P < 0.05 for changes in protein carbonylation values. Means with different capital letters are signi fi cantly different at P < 0.05 for changes in protein solubility values. Means with same letters are not signi fi cantly different (P > 0.05).
Figure 5 Evolution of protein solubility and global carbonylation in sarcoplasmic (a) and myo fi brillar (b) protein fractions during 165 days of frozen storage ( -10°C) in muscle of rainbow trout (Oncorhynchus mykiss) fed control (C) and essential oil (M) diets. The values corresponding to each time are expressed as fold change regarding to initial time (0 days). Means with different lowercase letters are signi fi cantly different at P < 0.05 for changes in protein carbonylation values. Means with different capital letters are signi fi cantly different at P < 0.05 for changes in protein solubility values. Means with same letters are not signi fi cantly different (P > 0.05).CC-BY-NC-ND · From the PDF
Figure 6 Water-holding capacity (WHC) during 165 days of frozen storage ( -10°C) in muscle of rainbow trout (Oncorhynchus mykiss) from control ( ● ) and essential oil ( ) diets. Means with different letters are signi fi cantly different at P < 0.05 among days of storage. Means with same letters are not signi fi cantly different (P > 0.05).
Figure 6 Water-holding capacity (WHC) during 165 days of frozen storage ( -10°C) in muscle of rainbow trout (Oncorhynchus mykiss) from control ( ● ) and essential oil ( ) diets. Means with different letters are signi fi cantly different at P < 0.05 among days of storage. Means with same letters are not signi fi cantly different (P > 0.05).CC-BY-NC-ND · From the PDF
Figure 7 Conjugated diene hydroperoxides (Hp, expressed as mmol Hp/kg lipid) (a), 2-thiobarbituric acid reactive substances (TBARS expressed as milligram of malondialdehyde (MDA-eq) equivalents/kg sample) (b) and increment of main volatiles (c) during 165 days of frozen storage ( -10°C), in muscle of rainbow trout (Oncorhynchus mykiss) fed control or essential oil diets. Means with different letters are signi fi cantly different at P < 0.05 among days of storage. Means with same letters are not signi fi cantly different (P > 0.05).
Figure 7 Conjugated diene hydroperoxides (Hp, expressed as mmol Hp/kg lipid) (a), 2-thiobarbituric acid reactive substances (TBARS expressed as milligram of malondialdehyde (MDA-eq) equivalents/kg sample) (b) and increment of main volatiles (c) during 165 days of frozen storage ( -10°C), in muscle of rainbow trout (Oncorhynchus mykiss) fed control or essential oil diets. Means with different letters are signi fi cantly different at P < 0.05 among days of storage. Means with same letters are not signi fi cantly different (P > 0.05).CC-BY-NC-ND · From the PDF

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Metadata

Authors
Santos, H. M. C., Méndez, L., Secci, G., Parisi, G., Martelli, R., & Medina, I.
ORCID
Méndez, L.
Venue
Animal
Publisher
Elsevier BV
Published
2019
Volume
13
Issue
9
Pages
2080-2091
ISSN
1751-7311
DOI
10.1017/s1751731119000016
Cited by
28
References
3
Language
en
Licence
Funders
Fondazione Edmund Mach

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Santos, H. M. C., Méndez, L., Secci, G., Parisi, G., Martelli, R., & Medina, I. (2019). Pathway-oriented action of dietary essential oils to prevent muscle protein oxidation and texture deterioration of farmed rainbow trout. Animal. https://doi.org/10.1017/s1751731119000016

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