Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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    Records 1 - 20 / 34

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    A global analysis on the energy content of the diet of the harbor porpoise (Phocoena phocoena)
    Hessing, S. ; Duchateau, M.J. ; Leopold, M.F. - \ 2019
    Dietary strategies to influence the gastrointestinal microflora of young animals, and its potential to improve intestinal health
    Snel, J. ; Harmsen, H.J.M. ; Wielen, P.W.J.J. van der; Williams, B.A. - \ 2002
    In: Nutrition and health in the gastrointestinal tract / Blok, M.C., Vahl, H.A., de Lange, L., van de Braak, A.E., Hemke, G., Hessing, M., Wageningen : Wageningen Academic Publishers - p. 37 - 69.
    Optimising nutrient digestion, absorption and gut barrier function in monogastrics: reality or illusion?
    Lange, L. de; Braak, A.E. van de; Hemke, G. ; Hessing, M. - \ 2002
    In: "Nutrition and health of the gastrointestinal tract" / Blok, M.C., Vahl, H.A., de Lange, L., van de Braak, A.E., Hemke, G., Hessing, M.,
    The interactions between feed (components) and Eimeria infections in poultry health
    Lange, L. de; Braak, A.E. van de; Hemke, G. ; Hessing, M. - \ 2002
    In: "Nutrition and health of the gastrointestinal tract" / Jeurissen, S.H.M., Veldman, B., Blok, M.C., Vahl, H.A.,
    Replacement of milk protein by vegetable protein in milk replacer diets for veal calves: digestion in relation to intestinal health
    Lange, L. de; Braak, A.E. van de; Hemke, G. ; Hessing, M. - \ 2002
    In: "Nutrition and health of the gastrointestinal tract" / Verdonk, J.M.A.J, Gerrits, W.J.J., Beynen, A.C., Blok, M.C., Vahl, H.A.,
    Soy Glycenin: Influence of pH and Ionic Strength on Solubility and Molecular Structure at Ambient Temperatures
    Lakemond, C.M.M. ; Jongh, H.H.J. de; Hessing, M. ; Gruppen, H. ; Voragen, A.G.J. - \ 2000
    Journal of Agricultural and Food Chemistry 48 (2000)6. - ISSN 0021-8561 - p. 1985 - 1990.
    soybean seeds - functional-properties - circular-dichroism - beta-conglycinin - gene - identification - subunits - proteins - globulin - purification
    This study describes the relationship between the solubility of glycinin, a major soy protein, and its structural properties at a quaternary, tertiary, and secondary folding level under conditions representative for food products. When the ionic strength is lowered from 0.5 to 0.2 or 0.03, the basic polypeptides shift more to the exterior of the glycinin complex, as determined at pH 7.6 by labeling solvent-exposed lysines, supported by the study of the proteolytic action of clostripain on glycinin. This structural reorganization caused the pH of minimal solubility to shift to higher values. Ultracentrifugational analysis shows that at pH 7.6 and an ionic strength of 0.5 glycinin forms hexameric complexes (11S), whereas at pH 3.8 and at an ionic strength of 0.03 glycinin exists as trimers (7S). Intermediate situations are obtained by modulation of pH and ionic strength. The observed quaternary dissociation correlates with an increased amount of nonstructured protein at a secondary level and with changes in tertiary folding as determined using circular dichroism. Tryptophan fluorescence shows no significant structural changes for different ionic strengths but demonstrates a more tightly packed fluorophore environment when the pH is lowered from 7.6 to 3.8.
    Peroxidase mediated cross-linking of proteins and carbohydrates to tailor their functional properties
    Oudgenoeg, G. ; Piersma, S. ; Boeriu, C. ; Gruppen, H. ; Hessing, M. ; Voragen, A.G.J. ; Laane, C. ; Hilhorst, R. - \ 2000
    Industrial Proteins 8 (2000). - ISSN 1381-0022 - p. 14 - 16.
    Heat denaturation of soy glycinin : Influence of pH and ionic strength on molecular structure
    Lakemond, C.M.M. ; Jongh, H.H.J. de; Hessing, M. ; Gruppen, H. ; Voragen, A.G.J. - \ 2000
    Journal of Agricultural and Food Chemistry 48 (2000). - ISSN 0021-8561 - p. 1991 - 1995.
    The 7S/11S glycinin equilibrium as found in Lakemond et al. (J. Agric. Food Chem. 2000, 48, xxxx-xxxx) at ambient temperatures influences heat denaturation. It is found that the 7S form of glycinin denatures at a lower temperature than the 11S form, as demonstrated by a combination of calorimetric (DSC) and circular dichroism (CD) experiments. At pH 7.6, at which glycinin is mainly present in the 11S form, the disulfide bridge linking the acidic and the basic polypeptides is broken during heat denaturation. At pH 3.8, at which glycinin has dissociated partly into the 7S form, and at pH 5.2 this disruption does not take place, as demonstrated by solubility and gel electrophoretic experiments. A larger exposure of the acidic polypeptides (Lakemond et al., 2000) possibly correlates with a higher endothermic transition temperature and with the appearance of an exothermic transition as observed with DSC. Denaturation/aggregation (studied by DSC) and changes in secondary structure (studied by far-UV CD) take place simultaneously. Generally, changes in tertiary structure (studied by near-UV CD) occur at lower temperatures than changes in secondary structure.
    Isolation and characterization of patatin isoforms
    Pots, A.M. ; Gruppen, H. ; Hessing, M. ; Boekel, M.A.J.S. van; Voragen, A.G.J. - \ 1999
    Journal of Agricultural and Food Chemistry 47 (1999). - ISSN 0021-8561 - p. 4587 - 4592.
    Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties
    Koppelman, S.J. ; Bruijnzeel-Koomen, C.A.F.M. ; Hessing, M. ; Jongh, H.H.J. de - \ 1999
    Journal of Biological Chemistry 274 (1999)8. - ISSN 0021-9258 - p. 4770 - 4777.
    Ara h 1, a major peanut allergen was isolated, and its structure on secondary, tertiary, and quaternary level at ambient temperature was investigated using spectroscopic and biochemical techniques. Ara h 1 appeared to be a highly structured protein on a secondary level, possesses a clear tertiary fold, and is present as a trimeric complex. Heat treatment of purified Ara h 1 results in an endothermic, irreversible transition between 80 and 90 degreesC, leading to an increase in beta-structures and a concomitant aggregation of the protein. Ara h 1 from peanuts that were heat-treated prior to the purification procedure exhibited a similar denatured state with an increased secondary folding and a decreased solubility. The effect of heat treatment on the in vitro allergenic properties of Ara h 1 was investigated by means of a fluid-phase IgE binding assay using serum from patients with a clinically proven peanut allergy. Ara h 1 purified from peanuts heated at different temperatures exhibited IgE binding properties similar to those found for native Ara h 1, indicating that the allergenicity of Ara h 1 is heat-stable. We conclude that the allergenicity of Ara h 1 is unaffected by heating, although native Ara h 1 undergoes a significant heat-induced denaturation on a molecular level, indicating that the recognition of conformational epitopes of Ara h 1 by IgE either is not a dominant mechanism or is restricted to parts of the protein that are not sensitive to heat denaturation.
    Heat induced conformational changes of Ara h 1, a major peanut allergen: effect on allergenic properties.
    Koppelman, S.J. ; Bruijnzeel-Koomen, C.A.F.M. ; Hessing, M. ; Jongh, H.H.J. de - \ 1998
    Journal of Biological Chemistry 273 (1998). - ISSN 0021-9258 - p. 4739 - 4741.
    The pH dependence of the structural stability of patatin.
    Pots, A.M. ; Jongh, H.H.J. de; Gruppen, H. ; Hessing, H. ; Voragen, A.G.J. - \ 1998
    Journal of Agricultural and Food Chemistry 46 (1998). - ISSN 0021-8561 - p. 2546 - 2553.
    Solubilisation and changes in molecular weight distribution of arabinoxylans and protein in wheat flours during bread-making, and the effects of endogenous arabinoxylan hydrolysing enzymes.
    Cleemput, G. ; Booij, C. ; Hessing, M. ; Gruppen, H. ; Delcour, J.A. - \ 1997
    Journal of Cereal Science 26 (1997). - ISSN 0733-5210 - p. 55 - 66.
    The specific-stress-free housing system has positive effects on productivity, health, and welfare of pigs
    Ekkel, E.D. ; Doorn, C.E.A. van; Hessing, M.J.C. ; Tielen, M.J.M. - \ 1996
    Journal of Animal Science 73 (1996)6. - ISSN 0021-8812 - p. 1544 - 1551.
    An experiment was conducted to determine the health, welfare, and growth performance of pigs housed under optimal climatic conditions in a Specific-Stress-Free (SSF) housing system. This system was compared to a conventional housing system with the same climatic conditions. Two identical experimental rooms with five pens each were used. In each room five litters were used for the experiments. The SSF pigs were not mixed or transported, whereas the pigs in the conventional housing system were mixed at weaning and mixed and transported at 25 kg. Average daily gain for the SSF pigs was higher (P < .05) both for the rearing period and for the finishing period (P < .01). Live weight at 143 d was, therefore, higher in the SSF group (95.09 kg vs 84.8 kg, P < .001). Clinical signs were hardly seen in the SSF group, but in the control group high levels of aggression after mixing caused ear, skin, and tail lesions. Cortisol concentration of the saliva was lower in SSF pigs after weaning (P < .01). Seven and 21 d after mixing, the SSF pigs had a higher response to an intradermal injection of phytohemagglutinin (P < .001) than the control pigs. In conclusion, production performance, health, and welfare are improved when pigs are kept in an SSF housing system where they are not mixed or transported.
    Isolation and characterization of the soy proteins glycinin and ß-conglycirin.
    Lakemond, C.M.M. ; Gruppen, H. ; Vliet, T. van; Hessing, M. - \ 1996
    In: VLAG Congr. Als speler op agro-food kennismarkt, Wageningen (1996) Ch.17
    Isolation, characterization and heat denaturation of soy glycinin and ß-conlycinin.
    Lakemond, C.C.M. ; Gruppen, H. ; Hessing, M. ; Vliet, T. van - \ 1996
    In: Non-Food Applications, Nantes, France - p. 179 - 179.
    Variation in the degree of D-xylose substitution in arabinoxylans extracted from a European wheat flour.
    Cleemput, G. ; Oort, M. van; Hessing, M. ; Bergmans, M.E.F. ; Gruppen, H. ; Grobet, P.J. ; Delcour, J.A. - \ 1995
    Journal of Cereal Science 22 (1995). - ISSN 0733-5210 - p. 73 - 84.
    Increased nitrogen secretion by inclusion of soya lectin in the diets of pigs.
    Schulze, H. ; Saini, H.S. ; Huisman, J. ; Hessing, M. ; Berg, W. van de; Verstegen, M.W.A. - \ 1995
    Journal of the Science of Food and Agriculture 69 (1995). - ISSN 0022-5142 - p. 501 - 510.
    Implications of individual behavioural characteristics on performance in pigs.
    Hessing, M.J.C. ; Schouten, W.G.P. ; Wiepkema, P.R. ; Tielen, M.J.M. - \ 1994
    Livestock Production Science 40 (1994). - ISSN 0301-6226 - p. 187 - 196.
    The effect of climatic environment and relocating and mixing on health status and productivity of pigs.
    Hessing, M.J.C. ; Tielen, M.J.M. - \ 1994
    Animal Production 59 (1994). - ISSN 0003-3561 - p. 131 - 139.
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