Effect of different extent of protein oxidation on the frozen storage stability of muscle protein in obscure pufferfish (Takifugu obscurus)
The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small piece...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Zheng, Yao [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2021transfer abstract |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Assessment of urban identity through a matrix of cultural landscapes - Ziyaee, Maryam ELSEVIER, 2017, an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST), Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:137 ; year:2021 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1016/j.lwt.2020.110416 |
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ELV052469778 |
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| 245 | 1 | 0 | |a Effect of different extent of protein oxidation on the frozen storage stability of muscle protein in obscure pufferfish (Takifugu obscurus) |
| 264 | 1 | |c 2021transfer abstract | |
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| 520 | |a The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. | ||
| 520 | |a The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. | ||
| 650 | 7 | |a Light exposure |2 Elsevier | |
| 650 | 7 | |a Oxygen concentration |2 Elsevier | |
| 650 | 7 | |a Water states |2 Elsevier | |
| 650 | 7 | |a Multiple freeze-thaw cycles |2 Elsevier | |
| 650 | 7 | |a Dorsal muscle |2 Elsevier | |
| 700 | 1 | |a Zhou, Fen |4 oth | |
| 700 | 1 | |a Zhang, Long |4 oth | |
| 700 | 1 | |a Wang, Hongli |4 oth | |
| 700 | 1 | |a Wang, Xi-chang |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Ziyaee, Maryam ELSEVIER |t Assessment of urban identity through a matrix of cultural landscapes |d 2017 |d an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) |g Amsterdam [u.a.] |w (DE-627)ELV004078675 |
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10.1016/j.lwt.2020.110416 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001565.pica (DE-627)ELV052469778 (ELSEVIER)S0023-6438(20)31404-3 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Zheng, Yao verfasserin aut Effect of different extent of protein oxidation on the frozen storage stability of muscle protein in obscure pufferfish (Takifugu obscurus) 2021transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. Light exposure Elsevier Oxygen concentration Elsevier Water states Elsevier Multiple freeze-thaw cycles Elsevier Dorsal muscle Elsevier Zhou, Fen oth Zhang, Long oth Wang, Hongli oth Wang, Xi-chang oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:137 year:2021 pages:0 https://doi.org/10.1016/j.lwt.2020.110416 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 137 2021 0 |
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10.1016/j.lwt.2020.110416 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001565.pica (DE-627)ELV052469778 (ELSEVIER)S0023-6438(20)31404-3 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Zheng, Yao verfasserin aut Effect of different extent of protein oxidation on the frozen storage stability of muscle protein in obscure pufferfish (Takifugu obscurus) 2021transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. Light exposure Elsevier Oxygen concentration Elsevier Water states Elsevier Multiple freeze-thaw cycles Elsevier Dorsal muscle Elsevier Zhou, Fen oth Zhang, Long oth Wang, Hongli oth Wang, Xi-chang oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:137 year:2021 pages:0 https://doi.org/10.1016/j.lwt.2020.110416 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 137 2021 0 |
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10.1016/j.lwt.2020.110416 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001565.pica (DE-627)ELV052469778 (ELSEVIER)S0023-6438(20)31404-3 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Zheng, Yao verfasserin aut Effect of different extent of protein oxidation on the frozen storage stability of muscle protein in obscure pufferfish (Takifugu obscurus) 2021transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. Light exposure Elsevier Oxygen concentration Elsevier Water states Elsevier Multiple freeze-thaw cycles Elsevier Dorsal muscle Elsevier Zhou, Fen oth Zhang, Long oth Wang, Hongli oth Wang, Xi-chang oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:137 year:2021 pages:0 https://doi.org/10.1016/j.lwt.2020.110416 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 137 2021 0 |
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10.1016/j.lwt.2020.110416 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001565.pica (DE-627)ELV052469778 (ELSEVIER)S0023-6438(20)31404-3 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Zheng, Yao verfasserin aut Effect of different extent of protein oxidation on the frozen storage stability of muscle protein in obscure pufferfish (Takifugu obscurus) 2021transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. Light exposure Elsevier Oxygen concentration Elsevier Water states Elsevier Multiple freeze-thaw cycles Elsevier Dorsal muscle Elsevier Zhou, Fen oth Zhang, Long oth Wang, Hongli oth Wang, Xi-chang oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:137 year:2021 pages:0 https://doi.org/10.1016/j.lwt.2020.110416 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 137 2021 0 |
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10.1016/j.lwt.2020.110416 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001565.pica (DE-627)ELV052469778 (ELSEVIER)S0023-6438(20)31404-3 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Zheng, Yao verfasserin aut Effect of different extent of protein oxidation on the frozen storage stability of muscle protein in obscure pufferfish (Takifugu obscurus) 2021transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. Light exposure Elsevier Oxygen concentration Elsevier Water states Elsevier Multiple freeze-thaw cycles Elsevier Dorsal muscle Elsevier Zhou, Fen oth Zhang, Long oth Wang, Hongli oth Wang, Xi-chang oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:137 year:2021 pages:0 https://doi.org/10.1016/j.lwt.2020.110416 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 137 2021 0 |
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effect of different extent of protein oxidation on the frozen storage stability of muscle protein in obscure pufferfish (takifugu obscurus) |
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Effect of different extent of protein oxidation on the frozen storage stability of muscle protein in obscure pufferfish (Takifugu obscurus) |
| abstract |
The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. |
| abstractGer |
The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. |
| abstract_unstemmed |
The objective of this study was to explore frozen storage stability of muscle protein of the obscure pufferfish using a semi-model system based on light exposure (LE), oxygen concentration (OC), and multiple freeze-thaw cycles (FTCs). The dorsal muscle of fifteen frozen fish was cut into small pieces (2 cm × 1.5 cm × 1 cm) and divided into 4 groups stored in differing conditions: one was stored in light with 0% oxygen (L-0), one in light with 20% oxygen (L-20), one in dark with 0% oxygen (D-0), and one in dark with 20% oxygen (D-20). All were subsequently subjected to five FTCs. Protein oxidation (PO) levels, protein structure, and water states were all assessed. The results showed that both LE and OC could significantly accelerate sulfhydryl and tryptophan loss, in the order of L-20 > L-0 and D-20 > D-0 during FTCs. Changes of protein structure were in line with the extent of PO indicated by surface hydrophobicity and UV absorbance. An increased PO also affected the water states, with higher PO resulting in immobilized water being more tightly trapped within the protein. However, thawing loss was shown to be independent of PO and the structural changes of myofibrillar protein. |
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Effect of different extent of protein oxidation on the frozen storage stability of muscle protein in obscure pufferfish (Takifugu obscurus) |
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