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Isolation and partial purification of mannose‐specific agglutinin from brewer's yeast involved in flocculation
Author(s) -
Straver Marika H.,
Traas Vincent M.,
Smit Gerrit,
Kijne Jan W.
Publication year - 1994
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320100906
Subject(s) - agglutinin , mannose , biology , flocculation , soybean agglutinin , yeast , lectin , biochemistry , wheat germ agglutinin , microbiology and biotechnology , chemistry , organic chemistry
Yeast cell‐agglutinating activity, designated agglutinin (possible lectin), was isolated from cell walls of both non‐flocculent and flocculent brewer's yeast cells. Agglutinin‐mediated aggregation of yeast cells in a manner similar to flocculation with respect to specific mannose‐sensitivity, pH‐dependence and calcium‐dependence. Agglutinating activity was found to be heat‐stable and protease‐insensitive. Furthermore, addition of agglutinin to flocculent cells strongly stimulated the flocculation ability of the cells, whereas addition to non‐flocculent cells rendered these cells weakly flocculent. Agglutinin was found to be released from flocculent cells during the course of a flocculation assay, but not from non‐flocculent cells. Presence of mannose during the assay inhibited release of agglutinin. Our results suggest that (i) mannose‐specific agglutinin is continuously synthesized during growth of brewer's yeast cells, (ii) agglutinin is present in cell walls of non‐flocculent cells but is unable to bind its ligand on other cells, and (iii) the ability of yeast cells to flocculate in a flocculation assay depends, among other factors, on release of agglutinin from the cells. A 10‐kDa polypeptide might represent one form of agglutinin.