The effect of cations on the hydrolysis of lactose and the transferase reactions catalysed by β-galactosidase from six strains of lactic acid bacteria

Garman, J.; Coolbear, Tim; Smart, James L.

doi:10.1007/s002530050778

Cited by 46 publications

(39 citation statements)

References 6 publications

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“…Various investigators reported that the activity of b-galactosidase was affected by metal ions (Reithel & Kim 1960;Garman et al 1996;Hung & Lee 2002;Kim et al 2003). Besides, it was reported that the ionic effects on the activity of b-galactosidase vary with substrates (Becker & Evans 1969).…”

Section: Discussionmentioning

confidence: 96%

“…Purification and characterization of b-galactosidase, obtained from various species of molds and bacteria, are also documented (Rohlfing & Crawford 1966;Somkuti & Steinberg 1979;Itoh et al 1980;Smart & Richardson 1987;Ohtsuka et al 1990;Dumortier et al 1994;Cavaille & Combes 1995;Garman et al 1996;Hung & Lee 2002). It has been shown that the properties of b-galactosidase varied with microorganisms.…”

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confidence: 96%

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Purification and characterization of a sodium-stimulated β-galactosidase from Bifidobacterium longum CCRC 15708

Hsu

Chou

2005

World J Microbiol Biotechnol

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b-galactosidase from Bifidobacterium longum CCRC 15708 was first extracted by ultrasonication then purified by Q Fast-Flow chromatography and gel chromatography on a Superose 6 HR column. These steps resulted in a purification of 15.7-fold, a yield of 29.3%, and a specific activity of 168.6 U mg )1 protein. The molecular weight was 357 kDa as determined from Native-PAGE. Using o-nitrophenyl-b-D-galactopyranoside (ONPG) as a substrate, the pH and temperature optima of the purified b-galactosidase were 7.0 and 50°C, respectively. The enzyme was stable at a temperature up to 40°C and at pH values of 6.5-7.0. K m and V max for this purified enzyme were noted to be 0.85 mM and 70.67 U/mg, respectively. Na + and K + stimulated the enzyme up to 10-fold, while Fe 3+ , Fe 2+ , Co 2+ , Cu 2+ , Ca 2+ , Zn 2+ , Mn 2+ and Mg 2+ inhibited the activity of b-galactosidase. Furthermore, although glucose, galactose, maltose, or raffinose exerted little or no effect on the b-galactosidase activity, lactose and fructose inhibited the enzyme activity. The effect of lactose on the enzyme activity for ONPG is probably a case of competitive inhibition.A relatively high specific activity of b-galactosidase from B. longum CCRC 15708 could be obtained by Q Fast-Flow chromatography and gel chromatography on a Superose 6 HR column. In some aspects, particularly the activation by monovalent cations, the properties of b-galactosidase of B. longum CCRC 15708 are different from those obtained from other sources.Data collected in the present study are of value and indispensable when b-galactosidase from B. longum CCRC 15708 is employed in practical application.

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Section: Discussionmentioning

confidence: 96%

mentioning

confidence: 96%

Purification and characterization of a sodium-stimulated β-galactosidase from Bifidobacterium longum CCRC 15708

Hsu

Chou

2005

World J Microbiol Biotechnol

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“…Also, several b-galactosidases from B. bifidum were found to display transferase activity [59,84,103,105,108]. Dumortier et al [59] purified a transgalactosidase and from a diversity of monomeric sugars only glucose and xylose could act as acceptors for transgalactosidase, using lactose as donor.…”

Section: B-galacto-oligosaccharidesmentioning

confidence: 99%

Bifidobacterium carbohydrases‐their role in breakdown and synthesis of (potential) prebiotics

Broek

Hinz

Beldman

et al. 2008

Molecular Nutrition Food Res

145

109

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There is an increasing interest to positively influence the human intestinal microbiota through the diet by the use of prebiotics and/or probiotics. It is anticipated that this will balance the microbial composition in the gastrointestinal tract in favor of health promoting genera such as Bifidobacterium and Lactobacillus. Carbohydrates like non-digestible oligosaccharides are potential prebiotics. To understand how these bacteria can grow on these carbon sources, knowledge of the carbohydrate-modifying enzymes is needed. Little is known about the carbohydrate-modifying enzymes of bifidobacteria. The genome sequence of Bifidobacterium adolescentis and Bifidobacterium longum biotype longum has been completed and it was observed that for B. longum biotype longum more than 8% of the annotated genes were involved in carbohydrate metabolism. In addition more sequence data of individual carbohydrases from other Bifidobacterium spp. became available. Besides the degradation of (potential) prebiotics by bifidobacterial glycoside hydrolases, we will focus in this review on the possibilities to produce new classes of non-digestible oligosaccharides by showing the presence and (transglycosylation) activity of the most important carbohydrate modifying enzymes in bifidobacteria. Approaches to use and improve carbohydrate-modifying enzymes in prebiotic design will be discussed.

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“…The covariate analysis showed no significant effect (P = 0.4478) of the initial β-gal activity in the CCEs on the kinetic parameters. Shah and Jelen [25] and Garman et al [6] also reported substantial differences in the β-gal activity in several different LAB species. The K m and k cat values obtained for the Lb11842 CCE in the present study were broadly similar to those determined by a different methodology for the same CCE preparation during lactose hydrolysis in 10% skim milk [33].…”

Section: Monosaccharide Formationmentioning

confidence: 99%

“…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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The effect of cations on the hydrolysis of lactose and the transferase reactions catalysed by β-galactosidase from six strains of lactic acid bacteria

Cited by 46 publications

References 6 publications

Purification and characterization of a sodium-stimulated β-galactosidase from Bifidobacterium longum CCRC 15708

Purification and characterization of a sodium-stimulated β-galactosidase from Bifidobacterium longum CCRC 15708

Bifidobacterium carbohydrases‐their role in breakdown and synthesis of (potential) prebiotics

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

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