A practical method for screening for beta-galactosidase secreting microbial colonies

Barreto, Eriana Serpa; Silva, Daison O.; Passos, Flávia Maria Lopes

doi:10.1590/s1517-83822000000100009

Cited by 3 publications

(3 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Peptone was the best nitrogen source for the production of β-galactosidase by strain B1.1. Our results agreed with those observed for Streptococcus thermophilus and Kluyveromyces lactis by Rao and Dutta [16] and Barreto et al [5], respectively, who demonstrated that peptone can be a good nitrogen source which that a maximum synthesis of β-galactosidase. On the other hand, these results were different from the report of Domingues et al [17] and Hsu et al [9], which indicated that the highest activity of this enzyme was obtained by Aspergillus niger and Bifidobacterium longum CCRC 15708, respectively, when using yeast extract.…”

Section: Effect Of Nitrogen Source On the Production Of β-Galactosidasesupporting

confidence: 93%

“…Lactose medium (0.5% lactose, 0.5% peptone, 0.3% beef extract, and 1.5% agar) was used in a plate-based screening of microorganisms aiming at the identification of strains producing thermophilic β-galactosidase activity. The ability of the different isolates to produce β-galactosidase was examined on lactose medium plates containing 50 μg mL -1 of 5-bromo-4chloro-3-idolyl-β-D-galactopyranoside (X-gal) as a chromogenic substrate and 1 mM of isopropyl β-D-1-thiogalactopyranoside (IPTG) as an additional inducer for the synthesis of β-galactosidase [5].…”

Section: Screening Of Microorganismsmentioning

confidence: 99%

See 1 more Smart Citation

Isolation and Production of Novel β-galactosidase from a Newly Isolated, Moderate Thermophile, Bacillus sp. Strain B1.1

Jaturapiree¹,

Phuengjayaeam²,

Seangsawang³

et al. 2012

JFSE

View full text Add to dashboard Cite

The enzyme β-galactosidase (lactase; EC 3.2.1.23) is a commercially important enzyme due to its various applications in dairy and food industries, which are based on the β-galactosidase-catalysed hydrolysis of lactose into glucose and galactose. The objectives of this work were to identify novel and attractive sources of this industrially relevant enzyme, and to study the effect of selected growth parameters (carbon source, lactose concentration, nitrogen source, peptone concentration, initial pH and temperature) on the formation of β-galactosidase. Based on a screening of isolates from Tha Pai hot spring, Mae Hong Son Province, Thailand, strain B1.1 was selected for further studies. Strain B1.1 is a Gram-positive, rod-shaped, catalase-positive bacterium that forms endospores. Based on the sequence of the 16S rDNA determined, this isolate is most closely related to Anoxybacillus sp. and Bacillus sp., and hence the strain is designated as Bacillus sp. B1.1. β-Galactosidase was produced by this strain with lactose and peptone as carbon and nitrogen sources, respectively. Optimal enzyme production occurred at an initial culture pH of 8.5 and at 45 °C. Under these optimum culture conditions, maximal volumetric and specific β-galactosidase activity of 0.478 U mL -1 and 0.338 U mg -1 protein, respectively, were obtained after 13 h of cultivation in a medium contain 2.5% lactose, 2.0% peptone, 0.3% K 2 HPO 4 , 0.1% KH 2 PO 4 and 0.05% MgSO 4 ·7H 2 O.

show abstract

Section: Effect Of Nitrogen Source On the Production Of β-Galactosidasesupporting

confidence: 93%

Section: Screening Of Microorganismsmentioning

confidence: 99%

Isolation and Production of Novel β-galactosidase from a Newly Isolated, Moderate Thermophile, Bacillus sp. Strain B1.1

Jaturapiree¹,

Phuengjayaeam²,

Seangsawang³

et al. 2012

JFSE

View full text Add to dashboard Cite

show abstract

“…The genus Kluyveromyces is utilized as a source of different enzymes, among which β-galactosidase (β-D-galactohydrolase, EC 3.2.1.23) (β-gal) (Barreto et al , 2000; Dagbagli and Goksungur, 2008) and inulinase (Jain et al , 2012). In particular, the species Kluyveromyces lactis can use lactose as the only carbon and energy source because of a high β-gal activity.…”

Section: Introductionmentioning

confidence: 99%

Statistical investigation of Kluyveromyces lactis cells permeabilization with ethanol by response surface methodology

Faria¹,

Rocha²,

Converti³

et al. 2013

Braz. J. Microbiol.

View full text Add to dashboard Cite

The aim of our study was to select the optimal operating conditions to permeabilize Kluyveromyces lactis cells using ethanol as a solvent as an alternative to cell disruption and extraction. Cell permeabilization was carried out by a non-mechanical method consisting of chemical treatment with ethanol, and the results were expressed as β-galactosidase activity. Experiments were conducted under different conditions of ethanol concentration, treatment time and temperature according to a central composite rotatable design (CCRD), and the collected results were then worked out by response surface methodology (RSM). Cell permeabilization was improved by an increase in ethanol concentration and simultaneous decreases in the incubation temperature and treatment time. Such an approach allowed us to identify an optimal range of the independent variables within which the β-galactosidase activity was optimized. A maximum permeabilization of 2,816 mmol L−1 oNP min−1 g−1 was obtained by treating cells with 75.0% v/v of ethanol at 20.0 °C for 15.0 min. The proposed methodology resulted to be effective and suited for K. lactis cells permeabilization at a lab-scale and promises to be of possible interest for future applications mainly in the food industry.

show abstract

New and simple plate test for screening relative transfructosylation activity of fungi

Dominguez

Santos

Teixeira

et al. 2006

Revista Iberoamericana de Micología

View full text Add to dashboard Cite

Several microorganisms are reported to have transfructosylation activity due to fructosyltransferase and/or fructofuranosidase activities. However, the search for other fungi with higher transfructosylation activity remains a challenge. So, a presumptive and indirect colorimetric plate assay for the evaluation of transfructosylation activity in fungi was developed which involved the simultaneous determination in the same plate of glucose and fructose released from sucrose. The method entailed the (a) glucose oxidase-peroxidase coupled reaction using phenol and 4-aminoantipyrine for determination of glucose; and (b) fructose dehydrogenase oxidation in the presence of a tetrazolium salt for determination of fructose. The presence of enzymes with transfructosylation activity was identified by the formation of pink (presence of glucose) and blue (presence of fructose) halos around the fungal colony. In conclusion, the results showed that the method is suitable for screening a large number of fungi due to its simplicity, reproducibility and rapidity and also gives a relative quantitative idea of the transfructosylation activity of different fungi species.

show abstract

A practical method for screening for beta-galactosidase secreting microbial colonies

Cited by 3 publications

References 6 publications

Isolation and Production of Novel β-galactosidase from a Newly Isolated, Moderate Thermophile, Bacillus sp. Strain B1.1

Isolation and Production of Novel β-galactosidase from a Newly Isolated, Moderate Thermophile, Bacillus sp. Strain B1.1

Statistical investigation of Kluyveromyces lactis cells permeabilization with ethanol by response surface methodology

New and simple plate test for screening relative transfructosylation activity of fungi

Contact Info

Product

Resources

About