Development of predictive modelling approaches for surface temperature and associated microbiological inactivation during hot dry air decontamination.

This research deals with the development of predictive modelling approaches in the field of heat transfer and microbial inactivation. Upon making some backstage microbiological considerations, surface temperature predictions during hot dry air decontaminations are incorporated in a microbial inactivation model, in order to describe inactivation kinetics under realistic (time-varying) temperature conditions. In the present study, the following parts are presented. (i) First, a one-dimensional heat transfer model is developed taking into account exchanges by convection, radiation and evaporation. The model is subsequently validated on a laboratory setup and on a test rig, assuming no water activity changes. This test rig is developed for studying-at a later stage-surface pasteurisation treatment on food products with the use of hot dry air. (ii) Isothermal inactivation data of Escherichia coli K12 MG1655 have been collected and inactivation parameters are accurately estimated by using a primary and a secondary model in a global modelling approach. (iii) Microbiological considerations such as microbial growth effects during come-up times, initial temperature of inactivation, and heat resistance effects, based on experimental observations and on literature studies, are formulated in order to evaluate possible microbial effects arising under the dynamic temperature conditions modelled in step (i). (iv) Microbial inactivation simulations with the incorporation of surface temperature predictions are presented. (v) Finally, the level of the microbial decontamination in an example based on the design of an industrial installation is presented, outlining the importance of the combination of surface temperature and microbial inactivation modelling approaches.

Generation of monoclonal antibodies against plant cell-wall polysaccharides. I. Characterization of a monoclonal antibody to a terminal alpha-(1-->2)-linked fucosyl-containing epitope.

Monoclonal antibodies (McAbs) generated against rhamnogalacturonan I (RG-I) purified from suspension-cultured sycamore maple (Acer pseudoplatanus) cells fall into three recognition groups. Four McAbs (group I) recognize an epitope that appears to be immunodominant and is present on RG-I from maize and sycamore maple, pectin and polygalacturonic acid from citrus, gum tragacanth, and membrane glycoproteins from suspension-cultured cells of maize, tobacco, parsley, bean, and sycamore maple. A second set of McAbs (group II) recognizes an epitope present in sycamore maple RG-I but does not bind to any of the other polysaccharides or glycoproteins recognized by group I. Lastly, one McAb, CCRC-M1 (group III), binds to RG-I and more strongly to xyloglucan (XG) from sycamore maple but not to maize RG-I, citrus polygalacturonic acid, or to the plant membrane glycoproteins recognized by group I. The epitope to which CCRC-M1 binds has been examined in detail. Ligand competition assays using a series of oligosaccharides derived from or related to sycamore maple XG demonstrated that a terminal alpha-(1-->2)-linked fucosyl residue constitutes an essential part of the epitope recognized by CCRC-M1. Oligosaccharides containing this structural motif compete with intact sycamore maple XG for binding to the antibody, whereas structurally related oligosaccharides, which do not contain terminal fucosyl residues or in which the terminal fucosyl residue is linked alpha-(1-->3) to the adjacent glycosyl residue, do not compete for the antibody binding site. The ligand binding assays also indicate that CCRC-M1 binds to a conformationally dependent structure of the polysaccharide. Other results of this study establish that some of the carbohydrate epitopes of the plant extracellular matrix are shared among different macromolecules.