Results 21 to 30 of about 57,026 (146)
Thermostable α-galactosidase fromThermotoga neapolitana: cloning, sequencing and expression [PDF]
FEMS Microbiology Letters, 1998 A gene encoding a thermostable alpha-galactosidase from the hyperthermophile Thermotoga neapolitana was cloned and sequenced. Sequence analysis showed that the 552-amino acid protein is similar to Escherichia coli Raf type alpha-galactosidase and belongs to Family 36 of the glycosyl hydrolases. Recombinant alpha-galactosidase expressed in E. coli has a
M R, King +3 more
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Journal of Basic and Applied Research in Biomedicine, 2022 Lactic acid bacteria (LAB) present in fermented foods has long been consumed by humans without any obvious adverse effects. Therefore, they are potent candidates as vehicles for the delivery of digestive enzymes.
Bhairav Prasad +2 more
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Yersinia pestis lacZexpresses a β-galactosidase with low enzymatic activity [PDF]
FEMS Microbiology Letters, 2006 Although very little, if any, beta-galactosidase activity is detected in Yersinia pestis by a standard Miller assay, we found that Y. pestis KIM6+ cells formed blue colonies on plates containing 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). Searches of the Y.
Alexander G, Bobrov, Robert D, Perry
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Purification and molecular properties of an α-galactosidase synthesized and secreted byAspergillus nidulans [PDF]
FEMS Microbiology Letters, 1993 alpha-Galactosidases from mycelial extract and culture filtrate of Aspergillus nidulans have been purified to homogeneity and utilised to obtain polyclonal antibodies anti-alpha-galactosidase. The enzymatic characteristics and the cross reactivity of the antibodies suggest that alpha-galactosidases isolated from the two sources were the same enzyme ...
S, Ríos +3 more
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A food-grade vector for Streptococcus thermophilus based on the α-complementation of β-galactosidase
Journal of Dairy Science, 2022 : Streptococcus thermophilus is a common yogurt starter that consumes lactose as its primary carbon source. The enzyme β-galactosidase is essential for the lactose metabolism and the growth of this species.
Z.S. Xu +5 more
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Expression of β-galactosidase inRhizobium japonicum [PDF]
FEMS Microbiology Letters, 1985 The plasmid pGC91.14 was used to introduce via conjugation the Escherichia coli lac operon into fast-growing and slow-growing strains of Rhizobium japonicum. Exconjugants now expressed higher levels of β-galactosidase activity which was still inducible by isopropyl-β-d-thiogalactoside (IPTG).
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Transcriptional analysis of the β-galactosidase gene (pbg) inClostridium perfringens [PDF]
FEMS Microbiology Letters, 1995 The mode of expression of the beta-galactosidase gene (pbg) of Clostridium perfringens was examined. The pbg gene was transcribed on a single 3.7-kb mRNA. The transcript contained a message for ORF54, located upstream of the pbg gene in the chromosome, indicating that ORF54 and the pbg gene comprise one operon (pbg operon). Expression of the pbg operon
T, Kobayashi, T, Shimizu, H, Hayashi
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Thermostable α-galactosidase fromBacillus stearothermophilusNUB3621: cloning, sequencing and characterization [PDF]
FEMS Microbiology Letters, 1999 An alpha-galactosidase gene from the thermophilic bacterium Bacillus stearothermophilus NUB3621 was cloned, sequenced, expressed in Escherichia coli and the recombinant protein was purified. The Bacillus enzyme, designated AgaN, is similar to alpha-galactosidases of family 36 in the classification of glycosyl hydrolases.
O, Fridjonsson +3 more
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Stability of native and modified α-galactosidase of Cladosporium cladosporioides [PDF]
The Ukrainian Biochemical Journal, 2015 By modifying carbohydrate component of glycoproteins it is possible to elucidate its role in manifestation of structural and functional properties of the enzyme. The comparison of activity and stability of the native and modified by oxidation with sodium
N. V. Borzova, L. D. Varbanets
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Anaerobic expression of thegyrAgene demonstrated by β-galactosidase activity ingyrA::Mu-lacfusion derivatives ofEscherichia coli [PDF]
FEMS Microbiology Letters, 1988 E. coli C600Δ lac was infected with a Mu- lac defective phage. Lysogens resistant to ampicillin (25 µg/ml) and nalidixic acid (20 µg/ml) were unable to grow anaerobically and insensitive to nalidixic acid (150 µg/ml), indicating formation of gyrA ::Mu- lac fusions.
Nobuto Yamamoto, Mary L. Droffner
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