Formation of oligosaccharides during enzymatic lactose: Part I: State of art

Prenosil, J. E.; Stuker, E.; Bourne, J.R.

doi:10.1002/bit.260300904

Cited by 159 publications

(93 citation statements)

References 32 publications

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“…On the other hand, GaOS production using ␤-GalI was increased 40-fold when the lactose concentration was increased from 1 to 20% (data not shown). The yield of GaOS by ␤-GalI was higher than those reported using the ␤-galactosidase of Thermus aquaticus (2), B. bifidum (10), Bacillus circulans (34), Aspergillus oryzae (44), and Kluyveromyces lactis (23), which were less than 42 mg/ml. The total concentration of GaOS (mainly tri-and tetrasaccharides) produced by the yeast Rhodotorula minuta ␤-galactosidase was about 78 mg/ml (40), which was lower than the total GaOS but higher than the concentration (66 mg/ml) of tri-and tetrasaccharides (Fig.…”

Section: Discussioncontrasting

confidence: 58%

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Molecular and Biochemical Analysis of Two β-Galactosidases fromBifidobacterium infantisHL96

Hung

Xia

et al. 2001

Appl Environ Microbiol

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Two genes encoding ␤-galactosidase isoenzymes, ␤-galI and ␤-galIII, from Bifidobacterium infantis HL96 were revealed on 3.6-and 2.4-kb DNA fragments, respectively, by nucleotide sequence analysis of the two fragments. ␤-galI (3,069 bp) encodes a 1,022-amino-acid (aa) polypeptide with a predicted molecular mass of 113 kDa. A putative ribosome binding site and a promoter sequence were recognized at the 5 flanking region of ␤-galI.

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Section: Discussioncontrasting

confidence: 58%

“…␤-Galactosidases (EC 3.2.1.23) catalyze both hydrolytic and transgalactosylation reactions (44,63). Hydrolytic activity has been applied in the food industry for decades for reducing lactose content in milk.…”

mentioning

confidence: 99%

Molecular and Biochemical Analysis of Two β-Galactosidases fromBifidobacterium infantisHL96

Hung

Xia

et al. 2001

Appl Environ Microbiol

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“…The linkage between the galactose units and the components in the final product depend on the enzymes and the conditions used in the reaction. The production and characterization of these TOS have been described in various publications (19,21,25). Different linkages between galactose and the reducing glucose (26,33).…”

mentioning

confidence: 99%

Characterization of a Novel β-Galactosidase from Bifidobacterium adolescentis DSM 20083 Active towards Transgalactooligosaccharides

Laere¹,

Abee

Schols³

et al. 2000

Appl Environ Microbiol

100

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This paper reports on the effects of both reducing and nonreducing transgalactooligosaccharides (TOS) comprising 2 to 8 residues on the growth of Bifidobacterium adolescentis DSM 20083 and on the production of a novel ␤-galactosidase (␤-Gal II). In cells grown on TOS, in addition to the lactose-degrading ␤-Gal (␤-Gal I), another ␤-Gal (␤-Gal II) was detected and it showed activity towards TOS but not towards lactose. ␤-Gal II activity was at least 20-fold higher when cells were grown on TOS than when cells were grown on galactose, glucose, and lactose. Subsequently, the enzyme was purified from the cell extract of TOS-grown B. adolescentis by anion-exchange chromatography, adsorption chromatography, and size-exclusion chromatography. ␤-Gal II has apparent molecular masses of 350 and 89 kDa as judged by size-exclusion chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, respectively, indicating that the enzyme is active in vivo as a tetramer. ␤-Gal II had an optimal activity at pH 6 and was not active below pH 5. Its optimum temperature was 35°C. The enzyme showed highest V max values towards galactooligosaccharides with a low degree of polymerization. This result is in agreement with the observation that during fermentation of TOS, the di-and trisaccharides were fermented first. ␤-Gal II was active towards ␤-galactosyl residues that were 134, 136, 133, and 171 linked, signifying its role in the metabolism of galactooligosaccharides by B. adolescentis.

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“…A minimum of three steps were involved, the last of which allows for hydrolysis or transferase activity [4,14]. It has been shown that trisaccharides dominated among various types of oligosaccharides [4,15,16] and the model can be simplified by considering only the production of trisaccharides [17]. But the mechanistic model is rather complex even when only trisaccharides are considered:…”

Section: Model Developmentmentioning

confidence: 99%

Experimental and Modeling Study of Galactosyl-Oligosaccharides Formation in Continuous Recycle Membrane Reactors (CRMR)

González¹,

Ebrahimi²,

Czermak³

2009

TOFSJ

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Galactosyl-oligosaccharides (GOS) can be produced with native enzymes in Continuous Recycle Membrane Reactors (CRMR) or with immobilized enzymes in Plug Flow Bed Reactors (PFBR). In this paper a simple three kinetic constants model was implemented and used to define the optimal operation conditions to obtain a higher GOS yield. Experimental GOS yield and productivity obtained with CRMR were in good agreement with simulated results. The advantages of using single CRMR, two coupled CRMR and single CRMR coupled with Simulated Moving Bed Chromatography (SMBC), for product separation and continuous lactose recycling, were investigated with a modeling and experimental study. Experimental studies for single CRMR showed a 89 % higher amount of produced GOS than reports from immobilized enzymes in Plug Flow Bed Reactors (PFBR). Two coupled CRMR produced a 25 % higher amount of GOS than single CRMR. Simulated results with CRMR and SMBC for continuous lactose recycling showed 45% higher GOS amount than single CRMR. The results prove the feasibility and advantages of GOS production in single or series CRMR with native enzymes with or without lactose recycling.

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Formation of oligosaccharides during enzymatic lactose: Part I: State of art

Cited by 159 publications

References 32 publications

Molecular and Biochemical Analysis of Two β-Galactosidases fromBifidobacterium infantisHL96

Molecular and Biochemical Analysis of Two β-Galactosidases fromBifidobacterium infantisHL96

Characterization of a Novel β-Galactosidase from Bifidobacterium adolescentis DSM 20083 Active towards Transgalactooligosaccharides

Experimental and Modeling Study of Galactosyl-Oligosaccharides Formation in Continuous Recycle Membrane Reactors (CRMR)

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