Casein Phosphopeptides from Casein Micelles by Successive Digestion with Pepsin and Trypsin | Zendy

Tomotada Ono | Zendy; Yasushi Takagi | Zendy; and Isao KUNISHI | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Casein Phosphopeptides from Casein Micelles by Successive Digestion with Pepsin and Trypsin

Author(s) -

Tomotada Ono,

Yasushi Takagi,

and Isao KUNISHI

Publication year - 1998

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.62.16

Subject(s) - trypsin , casein , pepsin , chemistry , micelle , chromatography , digestion (alchemy) , calcium , phosphate , biochemistry , enzyme , organic chemistry , aqueous solution

When milk is ingested, casein micelles will be successively digested by pepsin in the stomach and trypsin in the intestine. Therefore, we digested casein micelles successively with pepsin at pH 4.0 and trypsin at pH 7.0, and recovered casein phosphopeptides (CPP) as CPP-calcium phosphate (CP) complexes. The CPP-CP complexes contained 248 mg of calcium/g peptides and 175 mg of inorganic phosphorus/g peptides, which were higher than those of CPP-CP complexes driven from acid-precipitated casein and casein micelles by tryptic digestion only. It contained more alpha S1-CN-5P(f59-79) than the other CPP preparations did.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research