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|Title: ||Purification and identification of hypocholesterolemic peptides from freshwater clam hydrolysate with in vitro gastrointestinal digestion|
|Authors: ||Yu-Hsin Lin;Jenn-Shou Tsa;Guan-Wen Chen|
|Issue Date: ||2017-06-15T01:26:15Z
|Abstract: ||Abstract:The muscles of freshwater clams were extracted separately using hot water. Subsequently, the edible muscle part was freeze-dried, hydrolyzed at 50°C using Protamex to obtain the freshwater clam hydrolysate (PX), and then digested with pepsin. The bile-acid-binding capacity and inhibition of cholesterol micelle formation were subsequently investigated using pepsin-digested PX (PXP) through ultrafiltration (UF) fractionation or size exclusion chromatography. After the UF treatment, soluble protein (171.0 mg/g) and peptide (109.4 mg/g) contents in fraction III were found to be higher than those of all other membrane fractions. Assuming that bile acid binds to PXP at 100%, the relative bile-acid-binding capacities of fractions I, II, and III were 161.2%, 64.3%, and 55.1%, respectively. Fraction f showed the highest inhibitory efficiency ratio (IER), and its inhibition-peptide content percentage was 831.5% mg/mL. The amino acid sequences of two hypocholesterolemic peptides were Val–Lys–Pro and Val–Lys–Lys, with IERs of 64.8% and 10.2% mg/mL, respectively.|
|Appears in Collections:||[食品科學系] 期刊論文|
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