Identification and characterization of cryoprotective peptides extracted from silver carp (Hypophthalmichthys molitrix) hydrolysates
The cryoprotective effects on surimi matrix of hydrolysates with different hydrolyzing times prepared from silver carp using Protamex were compared with commercial sorbitol-sucrose cryoprotectants. Cryoprotective assays showed that FPH-30 (hydrolysate with 30 min hydrolyzing) was a more effective cr...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2019-01-01
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| Series: | International Journal of Food Properties |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/10942912.2019.1622563 |
| _version_ | 1818067317595045888 |
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| author | Qingjing Liu Yongle Liu Jian Yu Faxiang Wang Xianghong Li |
| author_facet | Qingjing Liu Yongle Liu Jian Yu Faxiang Wang Xianghong Li |
| author_sort | Qingjing Liu |
| collection | DOAJ |
| description | The cryoprotective effects on surimi matrix of hydrolysates with different hydrolyzing times prepared from silver carp using Protamex were compared with commercial sorbitol-sucrose cryoprotectants. Cryoprotective assays showed that FPH-30 (hydrolysate with 30 min hydrolyzing) was a more effective cryoprotectant than other hydrolysates, because the FPH-30 group displayed lower salt-soluble protein extractability loss (29.90 ± 0.84%), less actomyosin Ca2+-ATPase activity decrease (48.85 ± 2.56%) and unfrozen water content decrease (10.39 ± 0.63%) after six freeze-thaw cycles. To exploit industrial utilizations, FPH-30 was further purified with ultrafiltration membranes. The cryoprotective activity of the fraction (<3 kDa) was superior to the others by reducing the salt-soluble protein extractability loss (27.21 ± 0.98%) and impeding the actomyosin Ca2+-ATPase activity decrease (30.54 ± 1.21%). Mass spectrometry analysis showed that the fraction (<3 kDa) was mainly composed of three peptides of the sequences GVDNPGHPFIM(T) and IITNWDDMEK. The results clearly support that silver carp could be a potential source of cryoprotectant peptides for industrial applications. |
| first_indexed | 2024-12-10T15:21:46Z |
| format | Article |
| id | doaj.art-cbe6e8d9f3dc461aa279794c6b82b9f3 |
| institution | Directory Open Access Journal |
| issn | 1094-2912 1532-2386 |
| language | English |
| last_indexed | 2024-12-10T15:21:46Z |
| publishDate | 2019-01-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | International Journal of Food Properties |
| spelling | doaj.art-cbe6e8d9f3dc461aa279794c6b82b9f32022-12-22T01:43:39ZengTaylor & Francis GroupInternational Journal of Food Properties1094-29121532-23862019-01-012211011102310.1080/10942912.2019.16225631622563Identification and characterization of cryoprotective peptides extracted from silver carp (Hypophthalmichthys molitrix) hydrolysatesQingjing Liu0Yongle Liu1Jian Yu2Faxiang Wang3Xianghong Li4Changsha University of Science & TechnologyChangsha University of Science & TechnologyChangsha University of Science & TechnologyChangsha University of Science & TechnologyChangsha University of Science & TechnologyThe cryoprotective effects on surimi matrix of hydrolysates with different hydrolyzing times prepared from silver carp using Protamex were compared with commercial sorbitol-sucrose cryoprotectants. Cryoprotective assays showed that FPH-30 (hydrolysate with 30 min hydrolyzing) was a more effective cryoprotectant than other hydrolysates, because the FPH-30 group displayed lower salt-soluble protein extractability loss (29.90 ± 0.84%), less actomyosin Ca2+-ATPase activity decrease (48.85 ± 2.56%) and unfrozen water content decrease (10.39 ± 0.63%) after six freeze-thaw cycles. To exploit industrial utilizations, FPH-30 was further purified with ultrafiltration membranes. The cryoprotective activity of the fraction (<3 kDa) was superior to the others by reducing the salt-soluble protein extractability loss (27.21 ± 0.98%) and impeding the actomyosin Ca2+-ATPase activity decrease (30.54 ± 1.21%). Mass spectrometry analysis showed that the fraction (<3 kDa) was mainly composed of three peptides of the sequences GVDNPGHPFIM(T) and IITNWDDMEK. The results clearly support that silver carp could be a potential source of cryoprotectant peptides for industrial applications.http://dx.doi.org/10.1080/10942912.2019.1622563silver carp hydrolysatepeptidecryoprotective abilitysurimiidentification |
| spellingShingle | Qingjing Liu Yongle Liu Jian Yu Faxiang Wang Xianghong Li Identification and characterization of cryoprotective peptides extracted from silver carp (Hypophthalmichthys molitrix) hydrolysates International Journal of Food Properties silver carp hydrolysate peptide cryoprotective ability surimi identification |
| title | Identification and characterization of cryoprotective peptides extracted from silver carp (Hypophthalmichthys molitrix) hydrolysates |
| title_full | Identification and characterization of cryoprotective peptides extracted from silver carp (Hypophthalmichthys molitrix) hydrolysates |
| title_fullStr | Identification and characterization of cryoprotective peptides extracted from silver carp (Hypophthalmichthys molitrix) hydrolysates |
| title_full_unstemmed | Identification and characterization of cryoprotective peptides extracted from silver carp (Hypophthalmichthys molitrix) hydrolysates |
| title_short | Identification and characterization of cryoprotective peptides extracted from silver carp (Hypophthalmichthys molitrix) hydrolysates |
| title_sort | identification and characterization of cryoprotective peptides extracted from silver carp hypophthalmichthys molitrix hydrolysates |
| topic | silver carp hydrolysate peptide cryoprotective ability surimi identification |
| url | http://dx.doi.org/10.1080/10942912.2019.1622563 |
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