Author:
RECIO ISIDRA,AMIGO LOURDES,RAMOS MERCEDES,LOPEZ-FANDIÑO ROSINA
Abstract
Capillary electrophoresis using a hydrophilically coated capillary
and a
low pH buffer containing urea has been used to follow the proteolytic action
of
plasmin and chymosin on isolated casein fractions, whole casein and individual
milk
samples selected on the basis of their genetic variants. Several of the
main casein
breakdown products were identified. These included, among others,
γ1-casein (CN) A1,
γ1-CN A2,
γ1-CN B,
γ1-CN C,
γ2-CN A,
γ1-CN A3,
γ2-CN B,
γ3-CN A and
γ3-CN B, as well as proteose peptones, arising from the
action of plasmin on the
different genetic variants of β-CN. αs1-I-CN and
αs1-CN f(1-23) from αs1-CN, and
para-κ-CN and caseinomacropeptide from κ-CN produced by
chymosin action were
also separated. The knowledge of their migration times provided information
on the
extent and origin of casein hydrolysis in both milk and cheese, as found
in samples
of proteolysed milk or fresh cheese.
Publisher
Cambridge University Press (CUP)
Subject
Animal Science and Zoology,General Medicine,Food Science
Cited by
55 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献