Formation of Oligosaccharides During Hydrolysis of Lactose in Milk Using β‐Galactosidase from Bacillus circulans

Mozaffar, Zahid; Nakanishi, Kazuo; Matsuno, Ryuichi

doi:10.1111/j.1365-2621.1985.tb10543.x

Cited by 55 publications

(55 citation statements)

References 22 publications

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“…This lactose concentration was selected, considering further development of a continuous reactor, to assure good fluidity, thus minimizing clogging of the fixed bed. The GOS profile showed the typical pattern with a maximum GOS yield at approximately 50% of lactose conversion, followed by a progressive decrease of the GOS concentration [20]. The maximum GOS concentration was obtained at a similar lactose conversion as the soluble B. circulans β-galactosidase [18,19,21].…”

Section: Effect Of Lactose Conversion On Gos Yield With Immobilized Bmentioning

confidence: 84%

“…Compared with other β-galactosidases, this enzyme gives rise to a notable GOS yield (approximately 49% w/w, starting from 400 g/L lactose) [19]. In addition, it is appropriate for the dairy industry since it presents notable activity at pH 6.7 and is not inhibited by calcium [20]. Using milk as a substrate, the enzyme also displays a certain degree of transgalactosylation activity with a maximum GOS yield of 15% at approximately 50% lactose conversion [21].…”

Section: Immobilization Of β-Galactosidase From B Circulans On Glyoxmentioning

confidence: 99%

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Continuous Packed Bed Reactor with Immobilized β-Galactosidase for Production of Galactooligosaccharides (GOS)

et al. 2016

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Abstract:The β-galactosidase from Bacillus circulans was covalently attached to aldehyde-activated (glyoxal) agarose beads and assayed for the continuous production of galactooligosaccharides (GOS) in a packed-bed reactor (PBR). The immobilization was fast (1 h) and the activity of the resulting biocatalyst was 97.4 U/g measured with o-nitrophenyl-β-D-galactopyranoside (ONPG). The biocatalyst showed excellent operational stability in 14 successive 20 min reaction cycles at 45 • C in a batch reactor. A continuous process for GOS synthesis was operated for 213 h at 0.2 mL/min and 45 • C using 100 g/L of lactose as a feed solution. The efficiency of the PBR slightly decreased with time; however, the maximum GOS concentration (24.2 g/L) was obtained after 48 h of operation, which corresponded to 48.6% lactose conversion and thus to maximum transgalactosylation activity.HPAEC-PAD analysis showed that the two major GOS were the trisaccharide Gal-β(1→4)-Gal-β(1→4)-Glc and the tetrasaccharide Gal-β(1→4)-Gal-β(1→4)-Gal-β(1→4)-Glc. The PBR was also assessed in the production of GOS from milk as a feed solution. The stability of the bioreactor was satisfactory during the first 8 h of operation; after that, a decrease in the flow rate was observed, probably due to partial clogging of the column. This work represents a step forward in the continuous production of GOS employing fixed-bed reactors with immobilized β-galactosidases.

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Section: Effect Of Lactose Conversion On Gos Yield With Immobilized Bmentioning

confidence: 84%

Section: Immobilization Of β-Galactosidase From B Circulans On Glyoxmentioning

confidence: 99%

Continuous Packed Bed Reactor with Immobilized β-Galactosidase for Production of Galactooligosaccharides (GOS)

et al. 2016

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“…The formation of GaOS during lactose hydrolysis by ␤-galactosidases from yeast, bacteria, and fungi has been studied by several investigators (1,5,13,21,35,41,57,61). Those studies showed that the yields of GaOS were mainly affected by enzyme sources and substrate concentrations.…”

Section: Discussionmentioning

confidence: 99%

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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“…The transferase reactions have been described for highly purified β-gal preparations obtained from a number of microbial sources [6,11,20,27,29,31]. Using β-gal in the batch mode was suggested for maximization of oligosaccharide production [22].…”

Section: Introductionmentioning

confidence: 99%

Oligosaccharide production and proteolysis during lactose hydrolysis using crude cellular extracts from lactic acid bacteria

Vasiljevic

Jelen

2003

Lait

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-The extent of the lactose hydrolysis and oligosaccharide formation through transgalactosyl reactions by crude cellular extracts (CCE) containing intracellular β-galactosidase from disrupted Lactobacillus delbrueckii subsp. bulgaricus 11842, Lactobacillus delbrueckii subsp. lactis DMF 3078 or Streptococcus thermophilus 143 was investigated in lactose-containing buffered solutions or skim milk. Lactose hydrolysis was performed with lactose concentration ranging from 5 to 30% (w/w) at 30, 40, 50 or 60°C and terminated after 120 min. The proteolytic activities of the CCEs in skim milk systems were also assessed. All CCEs produced di-, tri-and tetrasaccharides in addition to monosaccharides as major products of the lactose hydrolysis in buffered lactose solutions. However, only Lb. lactis produced tetrasaccharides at detectable levels in skim milk preparations. The amount and the rate of oligosaccharide formation were significantly (P < 0.05) affected by the origin of the enzyme, lactose concentration and temperature. The maximum oligosaccharide production by all CCEs was reached at 50°C in 30% (w/w) lactose solution. St. thermophilus CCE produced significantly higher (P < 0.05) amounts of oligosaccharides than the other two CCE preparations at all lactose concentrations studied. However, Lb. bulgaricus CCE showed better lactose-hydrolyzing ability and higher proteolytic activity than the other two CCEs. The lactose hydrolysis generally proceeded faster at 50-60°C than at 30-40°C as opposed to the proteolytic maxima reached at 40°C.Crude cellular extract / β-galactosidase / thermophilic dairy culture / lactose hydrolysis / transferase reaction / proteolytic activity Résumé -Production d'oligosaccharides et protéolyse lors de l'hydrolyse de lactose par extraits cellulaires bruts de bactéries lactiques. Le degré d'hydrolyse du lactose et la formation d'oligosaccharides par réaction de transgalactosylation sous l'action d'extraits cellulaires bruts (ECB) contenant de la β-galactosidase obtenue par rupture de Lactobacillus delbruekii subsp. bulgaricus 11842, Lactobacillus delbruekii subsp. lactis DMF 3078 et Steptococcus thermophilus 143 ont été étudiés sur des solutions tamponnées de lactose ou sur le lait écrémé. L'hydrolyse du lactose a été effectuée sur des concentrations de 5 à 30 % (masse) à des températures de 30, 40, 50 et 60°C pour une durée totale de 120 min. L'activité protéolytique des ECBs sur les systèmes à base de lait écrémé a également été évaluée. Tous les ECBs ont produit des di-, tri-et tetrasaccharides en plus des monosaccharides comme composants majeurs de l'hydrolyse du lactose contenu dans les solutions tamponnées. Toutefois, seul Lb. lactis a produit des tetrasaccharides à un niveau * Corresponding author: paul.jelen@ualberta.ca 454 T. Vasiljevic, P. Jelen

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Formation of Oligosaccharides During Hydrolysis of Lactose in Milk Using β‐Galactosidase from Bacillus circulans

Cited by 55 publications

References 22 publications

Continuous Packed Bed Reactor with Immobilized β-Galactosidase for Production of Galactooligosaccharides (GOS)

Continuous Packed Bed Reactor with Immobilized β-Galactosidase for Production of Galactooligosaccharides (GOS)

Molecular and Biochemical Analysis of Two β-Galactosidases fromBifidobacterium infantisHL96

Oligosaccharide production and proteolysis during lactose hydrolysis using crude cellular extracts from lactic acid bacteria

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