Characterization of β-Galactosidase from Lactose Utilizing Yeast Isolated from the Dairy Sample
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چکیده
منابع مشابه
Production and Optimization of β-galactosidase by Bacillus Sp. MPTK 121, Isolated from Dairy Plant Soil
Studies on the β-galactosidase production were carried out with a bacterial strain isolated from the soil sample near dairy processing plant. The production of extracellular β-galactosidase by Bacillus sp. was optimized in a submerged fermentation. The effect of incubation period, temperature and pH of the medium were optimized. The production of the enzyme was found to be high at the 48th hour...
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The synthesis of galacto-oligosaccharides (GOS) catalyzed by a novel commercial preparation of β-galactosidase from Bacillus circulans (Biolactase) was studied, and the products were characterized by MS and NMR. Using 400 g/L lactose and 1.5 enzyme units per milliliter, the maximum GOS yield, measured by HPAEC-PAD analysis, was 165 g/L (41% w/w of total carbohydrates in the mixture). The majo...
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mouse genotyping by the three-primer multiple PCR. However, both of the smaller PCR products of 1068 (specific for the wild-type allele of mGluR4) and 1170 bp (specific for the mGluR4 transgene) were visible. Thus, all three allele combinations were clearly distinguishable on agarose gels stained with ethidium bromide. DNA from wildtype mice give a single smaller band (1068 bp; see Figure 2B, l...
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15 صفحه اولImmobilization of β-Galactosidase in Adsorptive Membranes for the Continuous Production of Galacto-Oligosaccharides from Lactose
A method for immobilization of β-galactosidase from Kluyveromyces lactis on an adsorptive membrane for the continuous synthesis of galacto-oligosaccharides from lactose was carried out. The immobilization was performed at 4, 10, 15 and 40°C. Two strongly basic anion exchange membranes with tradename MustangQ and SartobindQ were investigated. In static experiments, the highest enzyme activity wa...
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ژورنال
عنوان ژورنال: Tribhuvan University Journal of Microbiology
سال: 2020
ISSN: 2382-5499
DOI: 10.3126/tujm.v7i0.33874