A panel of 15 monoclonal antibodies (mAbs) has been raised to a fracti
on of lager beer protein precipitated with ammonium sulfate at 40% sat
uration. The antibodies have been characterized in terms of their bind
ing to a set of Octyl-Sepharose fractions of lager beer foam with incr
easing hydrophobicity (groups 1-5) by enzyme-linked immunosorbent assa
y and immunoblotting methods. The epitopes recognized were present in
all of the lager beer foam fractions to some degree, and many of the m
Abs bound to both high molecular mass (MM) (>3000 Da) and low MM (<300
0 Da) material. Two antibodies, IFRN 1612 and 1613, bound primarily to
the high MM material and preferentially recognized the more hydrophob
ic foam groups important in beer foam formation and stability. All of
the mAbs recognized proteins present in malt, with much of the binding
directed toward the material soluble in aqueous propanol from the hig
hly modified crystal malt used in the lager beer production. Such a li
brary of mAbs will be of use in investigating the contribution made by
proteins and derived polypeptides, such as those from malt, to qualit
y attributes such as foaming.