Searched for: subject%3A%22Glycosidase%22
(1 - 11 of 11)
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Adav, S.S. (author), Li, A.A. (author), Manavalan, A. (author), Punt, P. (author), Sze, S.K. (author), TNO Kwaliteit van Leven (author)
The natural lifestyle of Aspergillus niger made them more effective secretors of hydrolytic proteins and becomes critical when this species were exploited as hosts for the commercial secretion of heterologous proteins. The protein secretion profile of A. niger and its mutant at different pH was explored using iTRAQ-based quantitative proteomics...
article 2010
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Yuan, X.-L. (author), van der Kaaij, R.M. (author), van den Hondel, C.A.M.J.J. (author), Punt, P.J. (author), van der Maarel, M.J.E.C. (author), Dijkhuizen, L. (author), Ram, A.F.J. (author), TNO Kwaliteit van Leven (author)
The filamentous ascomycete Aspergillus niger is well known for its ability to produce a large variety of enzymes for the degradation of plant polysaccharide material. A major carbon and energy source for this soil fungus is starch, which can be degraded by the concerted action of α-amylase, glucoamylase and α-glucosidase enzymes, members of the...
article 2008
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Goosen, C. (author), van der Maarel, M.J.E.C. (author), Dijkhuizen, L. (author), TNO Kwaliteit van Leven (author)
The purified exo-inulinase enzyme of Aspergillus niger N402 (AngInuE; heterologously expressed in Escherichia coli) displayed a sucrose:inulin (S/I) hydrolysis ratio of 2.3, characteristic for a typical exo-inulinase. The enzyme also had significant transfructosylating activity with increasing sucrose concentrations, producing various...
article 2008
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Yuan, X.L. (author), Goosen, C. (author), Kools, H. (author), van der Maarel, M.J.E.C. (author), van den Hondel, C.A.M.J.J. (author), Dijkhuizen, L. (author), Ram, A.F.J. (author), TNO Kwaliteit van Leven (author)
As a soil fungus, Aspergillus niger can metabolize a wide variety of carbon sources, employing sets of enzymes able to degrade plant-derived polysaccharides. In this study the genome sequence of A. niger strain CBS 513.88 was surveyed, to analyse the gene/enzyme network involved in utilization of the plant storage polymer inulin, and of sucrose,...
article 2006
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TNO Kwaliteit van Leven TNO Voeding (author), Ozimek, L.K. (author), Kralj, S. (author), Kaper, T. (author), van der Maarel, M.J.E.C. (author), Dijkhuizen, L. (author)
Bacterial fructansucrase enzymes belong to glycoside hydrolase family 68 and catalyze transglycosylation reactions with sucrose, resulting in the synthesis of fructooligosaccharides and/or a fructan polymer. Significant differences in fructansucrase enzyme product specificities can be observed, i.e. in the type of polymer (levan or inulin)...
article 2006
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TNO Kwaliteit van Leven TNO Voeding (author), Kaper, T. (author), Talik, B. (author), Ettema, T.J. (author), Bos, H. (author), van der Maarel, M.J.E.C. (author), Dijkhuizen, L. (author)
Amylomaltases are 4-alpha-glucanotransferases (EC 2.4.1.25) of glycoside hydrolase family 77 that transfer alpha-1,4-linked glucans to another acceptor, which can be the 4-OH group of an alpha-1,4-linked glucan or glucose. The amylomaltase-encoding gene (PAE1209) from the hyperthermophilic archaeon Pyrobaculum aerophilum IM2 was cloned and...
article 2005
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TNO Voeding Centraal Instituut voor Voedingsonderzoek TNO (author), Ozimek, L.K. (author), van Hijum, S.A.F.T. (author), van Koningsveld, G.A. (author), van der Maarel, M.J.E.C. (author), van Geel-Schutten, G.H. (author), Dijkhuizen, L. (author)
Bacterial fructosyltransferases (FTFs) are retaining-type glycosidases that belong to family 68 of glycoside hydrolases. Recently, the high-resolution 3D structure of the Bacillus subtilis levansucrase has been solved [Meng, G. and Futterer, K., Nat. Struct. Biol. 10 (2003) 935-941]. Based on this structure, the catalytic nucleophile, general...
article 2004
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van der Maarel, M.J.E.C. (author), van der Veen, B. (author), Uitdehaag, J.C.M. (author), Leemhuis, H. (author), Dijkhuizen, L. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
Starch is a major storage product of many economically important crops such as wheat, rice, maize, tapioca, and potato. A large-scale starch processing industry has emerged in the last century. In the past decades, we have seen a shift from the acid hydrolysis of starch to the use of starch-converting enzymes in the production of maltodextrin,...
article 2002
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Montijn, R.C. (author), Vink, E. (author), Müller, W.H. (author), Verkleij, A.J. (author), van den Ende, H. (author), Henrissat, B. (author), Klis, F.M. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
β1,6-Glucan is a key component of the yeast cell wall, interconnecting cell wall proteins, β1,3-glucan, and chitin. It has been postulated that the synthesis of β1,6-glucan begins in the endoplasmic reticulum with the formation of protein-bound primer structures and that these primer structures are extended in the Golgi complex by two putative...
article 1999
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van den Berg, R.J.B.H.N. (author), Noort, D. (author), Milder-Enacache, E.S. (author), van der Marel, G.A. (author), van Boom, J.H. (author), Benschop, H.P. (author), Prins Maurits Laboratorium TNO (author)
In order to develop a generic treatment for infections with Gram- negative bacteria, we developed a synthesis of 2-acylamino-deoxynojirimycin derivatives (17, 18, 19 and 20), which will be used as haptens for raising catalytic antibodies capable of hydrolyzing the interglycosidic bond in the lipid A moiety of endotoxins. A key intermediate in...
article 1999
document
Gouka, R.J. (author), Hessing, J.G.M. (author), Punt, P.J. (author), Stam, H. (author), Musters, W. (author), van den Hondel, C.A.M.J.J. (author), TNO Voeding (author)
A new, highly inducible fungal promoter derived from the Aspergillus awamori 1,4-β-endoxylanase A (exlA) gene is described. Induction analysis, carried out with the wild-type strain in shake flasks, showed that exlA expression is regulated at the transcriptional level. Using a β-glucuronidase (uidA) reporter strategy, D-xylose was shown to be an...
article 1996
Searched for: subject%3A%22Glycosidase%22
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