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- W.G.B. Voorhorst (4)
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Characterisation and foaming properties of hydrolysates derived from rapeseed isolate
Larré, C. ; Mulder, W.J. ; Sánchez-Vioque, R. ; Lazko, J. ; Bérot, S. ; Guéguen, J. ; Popineau, Y. - \ 2006
Colloids and Surfaces. B: Biointerfaces 49 (2006)1. - ISSN 0927-7765 - p. 40 - 48.
brassica-napus l. - emulsifying properties - functional-properties - enzymatic-hydrolysis - beta-lactoglobulin - plant-proteins - peptides - gluten - albumin - whey
Two hydrolysis methods used to obtain rapeseed isolate derivates were compared: chemical hydrolysis performed under alkaline conditions and pepsic proteolysis performed under acidic conditions. The mean molecular weights obtained for the hydrolysates varied from 26 to 2.5 kDa, depending on the level of hydrolysis. Further characterisation showed that, at the same level of hydrolysis, the chemical hydrolysates differed by their charges and hydrophobicity from those derived from enzymatic digestion. Analysis of the foaming properties showed, for both cases, that a limited degree of hydrolysis, around 3%, was sufficient to optimise the foaming properties of the isolate despite the different physicochemical properties of the peptides generated. The study of foaming properties at basic, neutral and acidic pHs showed that the hydrolysate solutions yielded dense foams which drained slowly and which maintained a very stable volume under the three pH conditions tested.
Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
Oost, J. van der; Voorhorst, W.G.B. ; Kengen, S.W.M. ; Geerling, A.C.M. ; Wittenhorst, V. ; Gueguen, Y. ; Vos, W.M. de - \ 2001
European Journal of Biochemistry 268 (2001). - ISSN 0014-2956 - p. 3062 - 3068.
The gene encoding a short-chain alcohol dehydrogenase, AdhA, has been identified in the hyperthermophilic archaeon Pyrococcus furiosus, as part of an operon that encodes two glycosyl hydrolases, the -glucosidase CelB and the endoglucanase LamA. The adhA gene was functionally expressed in Escherichia coli, and AdhA was subsequently purified to homogeneity. The quaternary structure of AdhA is a dimer of identical 26-kDa subunits. AdhA is an NADPH-dependent oxidoreductase that converts alcohols to the corresponding aldehydes/ketones and vice versa, with a rather broad substrate specificity. Maximal specific activities were observed with 2-pentanol (46 U?mg1) and pyruvaldehyde (32 U?mg1) in the oxidative and reductive reaction, respectively. AdhA has an optimal activity at 90 °C, at which temperature it has a half life of 22.5 h. The expression of the adhA gene in P. furiosus was demonstrated by activity measurements and immunoblot analysis of cell extracts. A role of this novel type of archaeal alcohol dehydrogenase in carbohydrate fermentation is discussed.
|Transcriptional regulation in the hyperthermophilic archaeon Pyrococcus furiosus: Coordinated expression of divergently oriented genes in response to ß-linked glucose polymers
Voorhorst, W.G.B. ; Gueguen, Y. ; Geerling, A.C.M. ; Schut, G. ; Dahlke, I. ; Thomm, M. ; Oost, J. van der; Vos, W.M. de - \ 1999
Journal of Bacteriology 181 (1999)12. - ISSN 0021-9193 - p. 3777 - 3783.
|Modifications of wheat gluten for non-food applications
Graaf, L.A. de; Kolster, P. ; Vereijken, J.M. - \ 1998
In: 'Plant Proteins from European Crops' / Gueguen, J., Springer Verlag - p. 335 - 339.
|Molecular and biochemical characterization of anendo-(-1,3-glucanase of the hyperthermophilic archaeon Pyrococcus furiosus.
Gueguen, Y. ; Voorhorst, W.G.B. ; Oost, J. van der; Vos, W.M. de - \ 1997
Journal of Biological Chemistry 272 (1997). - ISSN 0021-9258 - p. 31258 - 31264.
|Molecular characterization of an endoglucanase from Pyrococcus furiosus.
Oost, J. van der; Gueguen, Y. ; Voorhorst, W.G.B. ; Vos, W.M. de - \ 1996
In: Abstracts 1st Int. Congr. on Extremophiles, Estoril, Portugal - p. 75 - 75.
Effects of a concentrate of pea antinutritional factors on pea protein digestibility in piglets.
Guen, M.P. le; Huisman, J. ; Gueguen, J. ; Beelen, G. ; Verstegen, M.W.A. - \ 1995
Livestock Production Science 44 (1995). - ISSN 0301-6226 - p. 157 - 167.