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  • 1
    Electronic Resource
    Electronic Resource
    Relation Between In Vitro Availability of Minerals and Food Composition: A Mathematical Model (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 58 (1993), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A mathematical model was developed to describe the relative influence of phytic acid, dietary fiber components, oxalic acid, citric acid and ascorbic acid on in vitro availability of Ca, Mg, Fe, Cu and Zn. The model was based on a combination of interdependent Langmuir isotherms. Throughout a diverse set of food products (cereal products, fruits, vegetables and nuts), the mathematical model described and predicted in vitro availability of Ca, Mg, Fe and Zn well (r = 0.89, 0.87, 0.90 and 0.92 respectively). The model proved valuable in studying simultaneous effects of food components on in vitm availability of minerals and trace elements in foods. Therefore, the mathematical model should help relate in vitro simulations to in vivo experiments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1993.tb06181.x
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  • 2
    Electronic Resource
    Electronic Resource
    The Use of Potato and Sweet Potato Starches Affects White Salted Noodle Quality (2003)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 68 (2003), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Potato and sweet potato starches and derivatives thereof were used to substitute part of the wheat flour in white salted noodle (WSN) manufacture. The quality of the WSN obtained was compared with the quality of WSN made from wheat flour only. When up to 20% of wheat flour was replaced by acetylated potato starch and acetylated sweet potato starches, the cooking loss of WSN decreased, while the softness, stretchability, and slipperiness increased significantly. Native and hydroxypropylated starches did not exhibit these effects. It can be concluded that the substitution of part of wheat flour with acetylated starches strongly affects noodle-making and final noodle quality, and starch substitution can be used to change the performance of a given wheat flour for noodle making in a desired way.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2003.tb05781.x
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  • 3
    Electronic Resource
    Electronic Resource
    Pektindepolymerasen I. Mitteilung Einteilung der Pektinsäuredepolymerasen nach ihrer Wirkung auf oligomere Galakturonsäuren (1970)
    Springer
    European food research and technology 142 (1970), S. 346-359 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Description / Table of Contents: Zusammenfassung Nach einer Besprechung der Einteilung der Pektindepolymerasen werden diejenigen Enzyme ausführlich besprochen, welche Pektinsäure abbauen und deren Wirkungsmechanismus auf Grund der Verwendung von Oligogalakturonsäuren als Substrat näher untersucht ist.
    Notes: Summary The general classification of pectindepolymerases is discussed. A review is given of work done on those pectic acid degrading enzymes the specific action of which has been studied by using oligogalacturonic acids as substrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01288221
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  • 4
    Electronic Resource
    Electronic Resource
    Degradation of different [(glucurono)arabino]xylans by a combination of purified xylan-degrading enzymes (1993)
    Springer
    Applied microbiology and biotechnology 38 (1993), S. 688-695 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The degradation of [({4-O-methyl-}glucurono)arabino]xylans from rice bran, oat spelts, wheat flour, larchwood, and birchwood with two types of endo-(1,4)-β-xylanase (I and III), (1,4)-β-xylosidase, (1,4)-β-d-arabinoxylan arabinofuranohydrolase (AXH), and an acetyl xylan esterase (AE), single and in combinations was investigated. The endo-(1,4)-β-xylanases showed the highest initial release of reducing end-groups on oat spelt xylan, followed successively by larchwood xylan, wheat flour xylan, birchwood xylan and rice bran xylan. The extent of degradation governed by degree and pattern of substitution was highest for oat spelts, followed by wheat flour and larchwood xylan. The extent of hydrolysis for the commercially available birchwood xylan was low, due to the partly insoluble fraction. Rice bran arabinoxylan could only partly be degraded by the combined action of endo-(1,4)-β-xylanase and AXH. The combination of endo-(1,4)-β-xylanase I or III, with (1,4)-β-xylosidase and AXH, or AE, resulted in the highest degree of hydrolysis after 24 h of incubation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00182811
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  • 5
    Electronic Resource
    Electronic Resource
    Rhamnogalacturonan acetylesterase: a novel enzyme from Aspergillus aculeatus, specific for the deacetylation of hairy (ramified) regions of pectins (1992)
    Springer
    Applied microbiology and biotechnology 38 (1992), S. 347-349 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Rhamnogalacturonan acetylesterase, able to specifically hydrolyse the acetyl asters present in modified hairy (ramified) regions (MHR) of apple pectin, was identified. The enzyme removed about 70% of the total acetyl groups in MHR. This acetylesterase did not cause the release of acetyl groups from a range of other acetylated substrates, either synthetic or extracted from plants, including the acetylated smooth regions present in beet pectin. Pretreatment of pectic polysaccharides in order to remove arabinose side chains had no effect on the acetyl release, wor was an effect found on the rate or degree of acetyl release, when the purified acetylesterase was combined with pectolytic enzymes, pectin methylesterase or arabinanases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00170084
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  • 6
    Electronic Resource
    Electronic Resource
    Purification and characterization of a (1,4)-β-d-arabinoxylan arabinofuranohydrolase from Aspergillus awamori (1991)
    Springer
    Applied microbiology and biotechnology 35 (1991), S. 753-758 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An enzyme able to split off arabinose sidechains from cereal arabinoxylans was isolated from a cell-free culture filtrate of Aspergillus awamori CMI 142717 containing milled oat straw as the carbon source. The enzyme was highly specific for arabinoxylans and, unlike other α-l-arabinofuranosidases reported in the literature, did not show any activity towards p-nitrophenyl α-l-arabinofuranoside, arabinans and arabinogalactans. This novel enzyme, which can be described as a (1,4)-β-d-arabinofuranohydrolase, had a molecular mass of 32 000 Da when determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and a specific activity of 22 units/mg on wheat arabinoxylan.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169890
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  • 7
    Electronic Resource
    Electronic Resource
    Purification and mode of action of two different arabinoxylan arabinofuranohydrolases from Bifidobacterium adolescentis DSM 20083 (1999)
    Springer
    Applied microbiology and biotechnology 51 (1999), S. 606-613 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Two novel arabinofuranohydrolases (AXH-d3 and AXH-m23) were purified from Bifidobacterium adolescentis DSM 20083. Both enzymes were induced upon growth of Bi. adolescentis on xylose and arabinoxylan-derived oligosaccharides. They were only active with arabinoxylans and therefore denoted as arabinoxylan arabinofuranohydrolases. Their optimal activity was at pH 6 and 30–40 °C. They were very specific in their mode of action and were clearly different from AXH-m from Aspergillus awamori. AXH-m23 released only arabinosyl groups, which were linked to the C-2 or C-3 position of singly substituted xylose residues in arabinoxylan oligomers. AXH-d3 hydrolysed C-3-linked arabinofuranosyl residues of doubly substituted xylopyranosyl residues of arabinoxylans and arab- inoxylan-derived oligosaccharides. No activity was observed with C-2-linked arabinofuranosyl residues of these doubly substituted xylopyranosyl residues, or against C-2- and C-3-linked arabinofuranosyl residues of singly substituted xylopyranosyl residues. The combination of AXH-d3 and AXH-m showed low debranching activity with highly substituted glucurono-arabinoxylans. However, arabinoxylan from wheat flour was debranched almost completely.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051439
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  • 8
    Electronic Resource
    Electronic Resource
    (1,4)-β-d-Arabinoxylan arabinofuranohydrolase: a novel enzyme in the bioconversion of arabinoxylan (1991)
    Springer
    Applied microbiology and biotechnology 35 (1991), S. 231-232 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An enzyme able to hydrolyse the terminal non-reducing α-l-arabinofuranoside residues from arabinoxylans only has been found. This enzyme was unable to split arabinofuranosyl linkages in a range of other arabinofuranosyl-containing substrates. Analysis of reaction mixtures of arabinoxylan with this enzyme did not show a shift in the molecular weight distribution of the arabinoxylan, even after 24 h of incubation. Only monomeric arabinose was released. 1H-Nuclear magnetic resonance studies of arabinoxylan treated with this enzyme, described as (1,4)-β-d-arabinoxylan arabinofuranohydrolase, indicated a specificity towards the single-substituted xylose in arabinoxylan.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00184692
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  • 9
    Electronic Resource
    Electronic Resource
    A new arabinofuranohydrolase from Bifidobacterium adolescentis able to remove arabinosyl residues from double-substituted xylose units in arabinoxylan (1997)
    Springer
    Applied microbiology and biotechnology 47 (1997), S. 231-235 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract An arabinofuranohydrolase (AXH-d3) was purified from a cell-free extract of Bifidobacterium adolescentis DSM 20083. The enzyme had a molecular mass of approximately 100 kDa as determined by gel filtration. It displayed maximum activity at pH 6 and 30 °C. Using an arabinoxylan-derived oligosaccharide containing double-substituted xylopyranosyl residues established that the enzyme specifically released terminal arabinofuranosyl residues linked to C-3 of double-substituted xylopyranosyl residues. In addition, this arabinofuranohydrolase released arabinosyl groups from wheat flour arabinoxylan polymer but showed no activity towards p-nitrophenyl α-l-arabinofuranoside or towards sugar-beet arabinan, soy arabinogalactan, arabino-oligosaccharides and arabinogalacto-oligosaccharides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050918
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  • 10
    Electronic Resource
    Electronic Resource
    Transglycosidase activity of Bifidobacterium adolescentis DSM 20083 α-galactosidase (1999)
    Springer
    Applied microbiology and biotechnology 52 (1999), S. 681-688 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Bifidobacterium adolescentis, a gram-positive saccharolytic bacterium found in the human colon, can, alongside other bacteria, utilise stachyose in vitro thanks to the production of an α-galactosidase. The enzyme was purified from the cell-free extract of Bi. adolescentis DSM 20083T. It was found to act with retention of configuration (α→α), releasing α-galactose from p-nitrophenyl galactoside. This hydrolysis probably operates with a double-displacement mechanism, and is consistent with the observed glycosyltransferase activity. As α-galactosides are interesting substrates for bifidobacteria, we focused on the production of new types of α-galactosides using the transgalactosylation activity of Bi. adolescentisα-galactosides. Starting from melibiose, raffinose and stachyose oligosaccharides could be formed. The transferase activity was highest at pH 7 and 40 °C. Starting from 300 mM melibiose a maximum yield of 33% oligosaccharides was obtained. The oligosaccharides formed from melibiose were purified by size-exclusion chromatography and their structure was elucidated by NMR spectroscopy in combination with enzymatic degradation and sugar linkage analysis. The trisaccharide α-d-Galp-(1 → 6)-α-d-Galp-(1 → 6)-d-Glcp and tetrasaccharide α-d-Galp-(1 → 6)-α-d-Galp-(1 → 6)-α-d-Galp-(1 → 6)-d-Glcp were identified, and this indicates that the transgalactosylation to melibiose occurred selectively at the C-6 hydroxyl group of the galactosyl residue. The trisaccaride α-d-Galp-(1 → 6)-α-d-Galp-(1 → 6)-d-Glcp formed could be utilised by various intestinal bacteria, including various bifidobacteria, and might be an interesting pre- and synbiotic substrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051579
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