Purification of Algal Calcium-Chelating Peptide and Its Physical Chemical Properties
| Autor: | Lingtuo Zhang, Yanlan Lin, Shaoyun Wang |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
chemistry.chemical_classification
Chromatography biology Size-exclusion chromatography chemistry.chemical_element Peptide 04 agricultural and veterinary sciences Schizochytrium Aquatic Science Calcium biology.organism_classification 040401 food science Hydrolysate Hydrolysis 0404 agricultural biotechnology chemistry Sephadex Peptide sequence Food Science |
| Zdroj: | Journal of Aquatic Food Product Technology. 27:518-530 |
| ISSN: | 1547-0636 1049-8850 |
| Popis: | The Schizochytrium protein, extracted from byproduct of Schizochytrium sp. after lipid extraction, was isolated and hydrolyzed. A specific calcium-binding peptide was purified from the hydrolysate through Sephadex G-25 gel filtration chromatography and C18 reversed-phase high-performance liquid chromatography (RP-HPLC). The calcium-binding capacity of the specific peptide reached up to 136.68 ± 4.6 μg/mg. The amino acid sequence was confirmed as Ser-Ser-Val (SSV) with a molecular weight of 291.15 Da by liquid chromatography electrospray ionization tandem mass spectrometry (LC–ESI–MS/MS). Fourier transformation infrared spectroscopy showed that the major binding sites included oxygen atom from carbonyl group and nitrogen of amino group or imino group. SSV-Ca chelate was confirmed to be a neutral molecular by Zeta potential analysis, and the calcium ion was surrounded by the functional chelating sites of SSV. In addition, thermogravimetry-differential scanning calorimetry (TG-DSC) and calcium releas... |
| Databáze: | OpenAIRE |
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