β-Galactosidase from Penicillium canescens. Properties and immobilization

Budrienė, Saulutė; Gorochovceva, Natalija; Romaskevic, Tatjana; Yugova, Lyubov V.; Mieželienė, Aldona; Dienys, Gervydas; Zubrienė, Asta

doi:10.2478/bf02476241

Cited by 26 publications

(11 citation statements)

References 13 publications

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“…Moreover, the recent interest in nanotechnology has provided a wealth of diverse nanoscaffolds that support its successful immobilization and improved stabilization on polyurethane powder [22], polyelectrolyte surfaces [23] and Al 2 O 3 nanoparticles [24].…”

Section: Discussionmentioning

confidence: 99%

Immobilization of Aspergillus oryzae β galactosidase on zinc oxide nanoparticles via simple adsorption mechanism

Husain

Ansari

Alam

et al. 2011

International Journal of Biological Macromolecules

139

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Section: Discussionmentioning

confidence: 99%

Immobilization of Aspergillus oryzae β galactosidase on zinc oxide nanoparticles via simple adsorption mechanism

Husain

Ansari

Alam

et al. 2011

International Journal of Biological Macromolecules

139

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“…Hsu et al [19] also showed that 1 mM of Mn 2+ lead to decreased β-galactosidase activity in B. longum CCRC 15708. Budriene et al [32] showed that β-galactosidase activity from Penicillium canescens was not sensitive to 1 mM of Na + , K + , Cu 2+ , Fe 2+ , Mn 2+ , and Mg 2+ ions in the growth culture.…”

Section: Induction Of β-Galactosidase By Different Metal Ionsmentioning

confidence: 98%

Enhancement of α- and β-Galactosidase Activity in Lactobacillus reuteri by Different Metal Ions

Ibrahim

Alazzeh

Awaisheh

et al. 2009

Biol Trace Elem Res

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The hydrolysis of oligosaccharides and lactose is of great importance to the food industry. Normally, oligosaccharides like raffinose, stachyose, and verbascose which are rich in different plants like soy bean are considered indigestible by the human gut. Moreover, many humans suffer from lactose intolerance due to the absence of effective enzyme that can digest lactose. alpha-Galactosidase can digest oligosaccharides like raffinose, while beta-galactosidases can hydrolyze lactose. Therefore, selection of microorganisms safe for human use and capable of producing high levels of enzymes becomes an attractive task. The objective of this study was to investigate the enhancement of alpha- and beta-galactosidase activity in Lactobacillus reuteri by different metal ions. Ten millimolar of Na(+), K(+), Fe(2+), and Mg(2+) and 1 mM of Mn(2+) were added separately to the growth culture of six strains of L. reuteri (CF2-7F, DSM20016, MF14-C, MM2-3, MM7, and SD2112). Results showed that L. reuteri CF2-7F had the highest alpha- and beta-galactosidase activity when grown in the medium with added Mn(2+) ions (22.7 and 19.3 Gal U/ml, respectively). 0.0274% of Mn(2+) ions lead to 27, 18% enhancement of alpha- and beta-galactosidase activity over the control group, and therefore, it could be added to the growth culture of CF2-7F to produce enhanced levels of alpha- and beta-galactosidase activity. The addition of Fe(2+) led to a significant (P < 0.01) decrease in the activity of both enzymes for most strains. This study shows that modified culture medium with that 0.0274% Mn(2+) can be used to promote the production for alpha- and beta-galactosidase in L. reuteri CF2-7F, which may lead to enhancement of alpha- and beta-galactosidase activity and have a good potential to be used in the food industry.

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“…Chitosan was activated with glutaraldehyde following a methodology adapted from Budriene et al [39]. The process was carried out by adding 5% (v/v) glutaraldehyde to 10 g of chitosan gel (10% w/v) at room temperature and pH 7.0 (phosphate buffer 100 mM).…”

Section: Chitosan-glutaraldehyde Activationmentioning

confidence: 99%

Immobilization and stabilization of an endoxylanase from Bacillus subtilis (XynA) for xylooligosaccharides (XOs) production

et al. 2016

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a b s t r a c tXylooligosaccharides (XOs) are small oligomers constituted by 2−10 units of xylan monomers, with important nutraceutical properties. They can be produced through hydrolysis of xylan catalyzed by an endoxylanase. The use of immobilized and stabilized enzymes may decrease the industrial process costs. In this study, XynA, a recombinant enzyme from B. subtilis, was immobilized in three different supports: agarose and chitosan activated with glyoxal groups and chitosan activated with glutaraldehyde. High immobilization yields were obtained, 100% for agarose-glyoxal and chitosan-glutaraldehyde, 82% for chitosan-glyoxal, with recovered activities of 42.7 (±1.3), 10.7 ± 0.8 and 53.6% (± 1.7), respectively. A great increase in the thermal stability of the enzyme (at 56 • C, pH 5.5) was achieved for the glyoxal derivatives: 75-fold for chitosan and 8600-fold for agarose. The great thermal stability obtained to the derivative agarose-glyoxal can be explained by the enzyme immobilization through lysine residues located in unstable sites of the protein structure. The agarose-glyoxal derivative was tested in the production of XOs (X2, X3 and X4) from soluble and conventional birchwood xylan, reaching approximately 20% of conversion in 3 h and 23% in 24 h, without the undesirable xylose production. After 10 cycles of hydrolysis, the conversion remained almost unchanged.

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β-Galactosidase from Penicillium canescens. Properties and immobilization

Cited by 26 publications

References 13 publications

Immobilization of Aspergillus oryzae β galactosidase on zinc oxide nanoparticles via simple adsorption mechanism

Immobilization of Aspergillus oryzae β galactosidase on zinc oxide nanoparticles via simple adsorption mechanism

Enhancement of α- and β-Galactosidase Activity in Lactobacillus reuteri by Different Metal Ions

Immobilization and stabilization of an endoxylanase from Bacillus subtilis (XynA) for xylooligosaccharides (XOs) production

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