  Various studies have shown that food structure has an impact on digestion
kinetics. We focus here on the effects of gastric and intestinal enzymes
(in-vitro digestion) on two canola seed storage proteins, napin and cruciferin.
To monitor structure effect we conducted experiments on gels of these proteins
at different pHs, yielding different structures and elastic modulus. What is
new is to get information on the mechanisms at the lowest scales, using imaging
and radiation scattering at large facilities: Synchrotron fluorescence
microscopy, X-Ray scattering, at SOLEIL synchrotron, and Small-Angle Neutron
Scattering, at Laboratoire L{\'e}on Brillouin reactor. We can identify the
mechanisms at each step and in two distinct scale ranges, observed
simultaneously, the one of the individual protein scale and the one of the
structure connectivity:-during gelation individual canola proteins are not
deeply modified in comparison with their state in solution ; larger scale gel
heterogeneity appears due to connectivity or aggregation-in the gastric step
(up to 40 min): o at short scale (large q) we see that the proteins
disintegration is much slowed down in gels than in solutions, particularly in
the gastric phase; o at larger scales (low q), we see that the gel structure is
also self-resistant to the action of the enzyme (pepsin).-in the intestinal
step, such kinetics differences hold until major disintegration after no more
than 15 min.
