Effects of<i>Botrytis</i><i>c</i><i>inerea</i>Infection on the Must Protein Electrophoretic Characteristics

Richard Marchal, Laurent Berthier, Laurent Legendre, L. Marchal-Delahaut, Philippe Jeandet, Alain Maujean

Journal of Agricultural and Food Chemistry · 1998 · 50 citations · 26 references

Concepts

Abstract

Qualitative effects of Botrytis cinerea infection on a must protein fraction were studied by comparing the electrophoretic patterns of musts obtained from healthy grapes or from grapes highly infected by B. cinerea . Evidence was obtained that proteins secreted by B. cinerea can degrade grape proteins. Most of the proteins present in the healthy must, between 20 and 30 kDa and a major glycoprotein at 62/64 kDa, disappeared in the infected must. Moreover an immunochemical technique, using polyclonal antibodies raised against B. cinerea -secreted proteins, was developed to specifically detect proteins originating from B. cinerea in the infected must. This is of particular interest when considering that some of the grape proteins participate in the foaming properties of Champagne wines. Keywords: Protein; must; Botrytis cinerea; antibodies; electrophoresis; proteolytic activity

References

26