Search Results

You are looking at 1 - 10 of 30 items for :

  • "β-galactosidase" x
Clear All

References Akcan , N. ( 2011 ): High level production of extracellular β-galactosidase from Bacillus licheniformis ATCC

Restricted access

. C HOONIA , H.S. & L ELE , S.S. ( 2013 ): Release of β-galactosidase by permeabilization of indigenously isolated Lactobacillus acidophilus using lysozyme . Chem. Biochem. Eng. Q. , 27 , 449 – 456

Restricted access

Andrews, K.P. & Li, S. (1994): Partial purification and characterization of β-galactosidase from sweet cherry, a nonclimacteric fruit. J. agric. Fd Chem. , 42 , 177

Restricted access

Carrington, C.M.S. & Pressey, R. (1996): β-Galactosidase II. activity in relation to changes in cell wall galactosyl composition during tomato ripening. J. Am. Soc. Hortic. Sci. , 121 , 132–136. Pressey

Restricted access

Sci. & Culture 1978 44 238 239 Bartley, I.M. (1974): β-Galactosidase

Restricted access
Acta Alimentaria
Authors: E. Kovács, P. Merész, Z. Kristóf and E. Németh-Szerdahelyi

Bartley, I.M. (1974): β-Galactosidase activity in ripening apples. Phytochemistry , 13 , 2107–2111. Bartley I.M. β-Galactosidase

Restricted access

. Statgraphics 5.1 (STSC) Bartley, I. M. (1974): β-Galactosidase activity in ripening apples. Phytochem. , 13 , 2107-2111. β-Galactosidase activity in ripening

Restricted access

. Alimenta 25 162 167 Bartley, I. M. (1974): β-Galactosidase activity in ripening apples. Phytochemistry , 13

Restricted access

Bartley, I. M. (1974): β-Galactosidase activity in ripening apples. Phytochemistry , 3 , 2107-2111. β-Galactosidase activity in ripening apples

Restricted access

We present a planar chromatographic separation method for the phytoestrogenic active compound equol, separated on RP-18 W (Merck, 1.14296) phase. It could be shown that an ethanolic cattle manure extract contains this phytoestrogenic active compound to a larger amount. As solvents for the mobile phase, hexane, ethyl acetate, and acetone (45:15:10, v/v); acetone and water (15:10, v/v); and n-hexane, CH2Cl2, ethyl acetate, methanol, and formic acid (40:40:20:5:1, v/v) have been used. After separation, a modified yeast estrogen screen (YES) test was applied, using the yeast strain Saccharomyces cerevisiae BJ3505 containing an estrogen receptor. Its activation by equol induces the reporter gene lacZ which encodes the enzyme β-galactosidase. The enzyme activity is measured directly on the TLC plate by using the substrate MUG (4-methylumbelliferyl-β-d-galactopyranoside) or the substrate X-β-Gal (5-bromo-4-chloro-3-indoxyl-β-d-galactopyranoside). β-Galactosidase cleaves MUG into a fluorescing compound. X-β- Gal is also hydrolyzed and then oxidized by oxygen forming the deep-blue dye 5,5′-dibromo-4,4′-dichloro-indigo. Both reactions in combination with a thin-layer chromatography (TLC) separation allow very specific detecting of equol in cattle manure, although that is a very challenging matrix. Preliminary results show that the average content of equol in liquid manure is roughly 60 μg g−1. The value for urine is 50 μg mL−1.

Restricted access