Coupled Neutrase–Catalyzed Plastein Reaction Mediated the ACE-Inhibitory ActivityIn Vitroof Casein Hydrolysates Prepared by Alcalase
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چکیده
منابع مشابه
Properties of Casein Hydrolysate as Affected by Plastein Reaction in Ethanol-Water Medium
Zhang Y., Zhao X.-H. (2013): Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium. Czech J. Food Sci., 31: 559–567. Casein hydrolysate with in vitro ACE-inhibitory activity of 44.4% at 0.3 mg/ml was generated from casein by Alcalase and modified by the Alcalase-catalysed plastein reaction in an ethanol-water medium. Eight treated hydrolysates were prepared u...
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Papain was used to prepare a casein hydrolysate with a degree of hydrolysis of 9.4 %. The hydrolysate had the in vitro antioxidant activity with a DPPH radical scavenging activity of 38.7 % and an EC50 of 1.63 mg/mL. Extrinsic phenylalanine or tyrosine was added to the hydrolysate for a papain-catalyzed plastein reaction. The temperature, substrate mass per volume fraction, and the levels of en...
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Casein is almost insoluble at around pH 4.6, which is its isoelectric point (pI). Grafting copolymer, casein-g-dextran, was prepared through the Amadori rearrangement of the Maillard reaction. The copolymer has a reversible pH sensitive property: micellization at the pI of casein forming a casein core and dextran shell structure and dissociation when pH differs from the pI. The micelles produce...
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The objectives of the present study were two-fold: first, to detect whether salmon protein fractions possess angiotensin I-converting enzyme (ACE) inhibitory properties and whether salmon proteins can release ACE inhibitory peptides during a sequential in vitro hydrolysis (with commercial porcine enzymes) and ex vivo digestion (with human gastrointestinal enzymes). Secondly, to evaluate the ACE...
متن کاملAnalysis of Peptide Profiles of Casein Hydrolysates Prepared with Pepsin, Trypsin and Subtilisin
Aiming the use of protein hydrolysates for dietetic purposes, casein was hydrolysed by using pepsin (P), isolated and in association with trypsin (T) and subtilisin (S). Sixteen hydrolysates were prepared and their peptide profiles were characterized. The hydrolysates were fractionated by size-exclusion HPLC, and the rapid Correct Fraction Area method was used for quantifying peptides and free ...
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ژورنال
عنوان ژورنال: International Journal of Food Properties
سال: 2013
ISSN: 1094-2912,1532-2386
DOI: 10.1080/10942912.2011.553759