High gene expression inEscherichia coliof recombinant alginate lyase as a fused protein with β-galactosidase α-peptide [PDF]
Escherichia coli LE392 (pAL28) was previously isolated as a positive clone harboring the alginate lyase gene (aly) from an alginate-degrading strain, Pseudomonas sp. OS-ALG-9. The plasmid pAL205, one of the constructs obtained after successive subcloning of pAL28, gave the highest expression of aly in E. coli cells.
K, Fujiyama +3 more
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Lactobacillus fermentumCRL 722 is able to deliver active α-galactosidase activity in the small intestine of rats [PDF]
alpha-galactooligosaccharides (alpha-GOS) found in legumes such as soybeans can cause gastrointestinal disorders since mammals lack alpha-galactosidase (alpha-Gal) in the small intestine which is necessary for their hydrolysis. Lactobacillus fermentum CRL 722 is a lactic acid bacterium (LAB) capable of degrading alpha-GOS due to its elevated alpha-Gal ...
Leblanc, Jean Guy +3 more
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Insertion of a 27 amino acid viral peptide in different zones ofEscherichia coliβ-galactosidase: Effects on the enzyme activity [PDF]
Seven internal, putatively exposed regions of Escherichia coli beta-galactosidase have been explored regarding their tolerance to insertions of large foreign peptides. Small sequence modifications, including amino acid substitutions and small deletions, were introduced into the lacZ gene to generate unique BamHI restriction sites. By using these mutant
A, Benito, A, Villaverde
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Lactobacillus delbrueckii subsp. bulgaricus 11842 (LB 11842) was grown in reconstituted sweet whey supplemented with 0 to 1% yeast extract. The β-galactosidase activity was determined from the hydrolysis of o-nitrophenyl- β-D-galactopyranoside (ONPG) by ...
D. Bury, J. Geciova, P. Jelen
doaj +1 more source
Cloning and characterization of a novel α-galactosidase fromBifidobacterium breve203 capable of synthesizing Gal-α-1,4 linkage [PDF]
A novel alpha-galactosidase gene (aga2) was cloned from Bifidobacterium breve 203. It contained an ORF of 2226-bp nucleotides encoding 741 amino acids with a calculated molecular mass of 81.5 kDa. The recombinant enzyme Aga2 was heterogeneously expressed, purified and characterized. Regarding substrate specificity for hydrolysis, Aga2 was highly active
Han, Zhao +8 more
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Isolation and Identification of Beta-galactosidase Producing Yeasts From Some Dairy Products [PDF]
Twenty-two β-galactosidase-producing yeast isolates were isolated from local dairy products. The purified isolates were evaluated for their β-galactosidase activity to identify the most productive isolates for subsequent investigations. The isolates were
Magda Abdalla +4 more
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Identification of bacteria with β-galactosidase activity in faeces from lactase non-persistent subjects [PDF]
Previous studies suggest that, besides the maldigestion of lactose in the small intestine, the colonic processing of lactose might play a role in lactose intolerance. beta-Galactosidase is the bacterial enzyme which catalyzes the first step of lactose fermentation in the colon.
Tao, H +3 more
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: β-Galactosidase is one of the most important enzymes used in dairy processing. It converts lactose into glucose and galactose, and also catalyzes galactose to form galactooligosaccharides (GOS), so-called prebiotics.
J.C. Zhao +5 more
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α-Galactosidase A fromPseudomonas fluorescenssubsp.cellulosa: cloning, high level expression and its role in galactomannan hydrolysis [PDF]
A library of Pseudomonas fluorescens subsp. cellulosa genomic DNA, constructed in lambda ZAPII, was screened for alpha-D-galactosidase activity. The DNA inserts from six galactosidase-positive clones were rescued into plasmids. Restriction digestion and Southern analysis revealed that each of the plasmids contained a common DNA sequence.
J R, Halstead +5 more
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The current study was undertaken to immobilize Kluveromyces lactis β-galactosidase on alginate coated magnesium oxide nanoparticles (ACMONPs). Transmission electron microscopy showed that MgO-NPs synthesized by wet chemical approach were of 27 nm size ...
Shakeel Ahmed Ansari +3 more
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