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Preparation and characterisation of an easily absorbabl Mg‐casein hydrolysate complex produced through enzymatic hydrolysis and ultrafiltration
Author(s) -
Hong HyeJin,
Kim Enjin,
Park InSu,
Ryu JungHo,
Ryu Taegong,
Kim ByoungGyu,
Chung KangSup
Publication year - 2015
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.12650
Subject(s) - hydrolysate , chemistry , casein , papain , chromatography , hydrolysis , ultrafiltration (renal) , trypsin , chelation , substrate (aquarium) , bioavailability , enzymatic hydrolysis , enzyme , biochemistry , organic chemistry , biology , bioinformatics , ecology
Summary In this study, we synthesised a Mg‐casein hydrolysate complex that allowed the effective absorption of Mg. The type of enzyme (papain, alcalase 2.4 L, pepsin, trypsin) and the enzyme/substrate ratio for casein hydrolysis was optimised. When the enzyme/substrate ratio was 30%, the alcalase 2.4 L‐hydrolysate showed the highest Mg‐chelation efficiency, of 96.1%. To characterise and enhance the function of casein hydrolysate, we fractionated the casein hydrolysate according to molecular weight using ultrafiltration. The Mg‐chelation efficiency was increased with the decrease in the molecular‐weight range of the hydrolysate fractions. The smallest casein hydrolysate (fraction 5, 1 kDa<) is used for preparation of Mg‐casein hydrolysate complex. Synthesised Mg‐casein hydrolysate complex (fraction 5) exhibited 100% Mg solubility and 39.5% Mg bioavailability. These results indicated that the Mg‐casein hydrolysate remained a stable chelate during simulated gastro‐intestinal digestion in vitro . The Mg‐casein hydrolysate complex exhibited excellent antioxidant activity as well as Mg binding.