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1

Alpha-galactosidase in immobilized cells of Citrullus vulgaris L.

100%
Stano J., Micieta K., Tokhtaeva E., Fulmekova M.
Herba Polonica
|
2005
|
tom 51
|
nr 3-4
Cells of suspension culture Citrullus vulgaris cv. "Samara" were permeabilized by Tween 80 and immobilized by glutaraldehyde. The highest a-galactosidase activity was at pH 5.4 and 60°C. The hydrolysis of substrate was linear for 3.5 h reaching 65-70% conversion of the substrate. The cells characterized with high enzyme activity, and stability in long-term storage showed convenient physico-mechanical properties (physical protection from shear forces and easy separation of product from biocatalysts).
2

Optimization of alpha-galactosidase production in Streptomyces erythrus

88%
Elshafei A. M., Foda M. S., Abdel-Mobde E., Ali N. H.
Acta Microbiologica Polonica
|
2001
|
tom 50
|
nr 1
3

Changes in the activity of alpha-galactosidase and alpha-L-fucosidase during the posthatch development and regression of Japanese quail testes and epididymis after light reduction

75%
Jozefczyk R., Droba M., Droba B.
Annals of Animal Science
|
2008
|
tom 08
|
nr 1
47-56
4

Purification and some properties of alpha-galactosidase from Mortierella vinacea IBT-3

75%
Galas E., Miszkiewicz H.
Acta Microbiologica Polonica
|
1996
|
tom 45
|
nr 2
5

Purification and properties of alpha-galactosidase isozymes from Phlebia radiata

75%
Prendecka M., Szyjka K., Rogalski J.
Acta Microbiologica Polonica
|
2003
|
tom 52
|
nr 1
6

Immune modulation in xenotransplantation

63%
Boksa M., Zeyland J., Slomski R., Lipinski D.
Archivum Immunologiae et Therapiae Experimentalis
|
2015
|
tom 63
|
nr 3
7

Double transgenic pigs with combined expression of human alpha1,2-fucosyltransferase and alpha-galactosidase designed to avoid hyperacute xenograft rejection

63%
Zeyland J., Wozniak A., Gawronska B., Juzwa W., Jura J., Nowak A., Slomski R., Smorag Z., Szalata M., Mazurek U., Lipinski D.
Archivum Immunologiae et Therapiae Experimentalis
|
2014
|
tom 62
|
nr 5
8

The effect of recombinant human alpha-1,2-fucosyltransferase and alpha-galactosidase A on the reduction of alpha-gal expression in the liver of transgenic pigs

63%
Wiater J., Karasinski J., Slomski R., Smorag Z., Wartalski K., Gajda B., Jura J., Romek M.
Folia Biologica
|
2020
|
tom 68
|
nr 4
9

Glycosidases and acid-invertase activities are not correlated with Phaseolus hypocotyl growth

63%
Bagatharia S. B., Chanda S. V.
Acta Physiologiae Plantarum
|
1998
|
tom 20
|
nr 4
Changes in α-galactosidase, β-galactosidase, β-glucosidase and acid invertase activities were examined in Phaseolus vulgaris hypocotyls treated with gibberellic acid (GA), naphthyl acetic acid (NAA) and distilled water (DW) (control) in light condition. The activities were estimated both in cytoplasmic and ionically wall-bound fraction. The upper segment showed considerable elongation growth while there was hardly any growth in lower segment. GA and NAA showed distinct promotion and inhibition respectively in hypocotyl growth in upper segment. The glycosidase activities were detected in both the fractions but the activity was more pronounced in cytoplasmic than in wall fraction. Acid invertase activity was present only in cytoplasmic fraction. In lower segment, in both cytoplasmic and wall fraction, the glycosidase activity, in general, showed a decreasing trend and no effect of treatment could be envisaged. In upper segment, though the trend was similar to the lower one, in α- and β-galactosidase NAA treated segment had more activity. Invertase activity also did not show a clear trend to implicate its function in hypocotyl elongation growth. The results are discussed in relation to establishing a correlation between an activity (glycosidase and invertase) and a physiological process (hypocotyl elongation). It is concluded that these wall-loosening enzymes have no role in elongation growth of Phaseolus vulgaris hypocotyls.
10
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Acid alpha-galactosidase is involved in D-chiro-inositol accumulation during tartary buckwheat germination

51%
Jia C.-F., Hu W.-H., Chang Z., Gao H.-L.
Acta Societatis Botanicorum Poloniae
|
2015
|
tom 84
|
nr 1
Tartary buckwheat seed and especially its sprouts are rich in D-chiroinositol (DCI). The research was to evaluate when DCI was most accumulated in tartary buckwheat sprouts. In addition, we explored the activity and expression pattern of α-galactosidase during tartary buckwheat seed germination. The results showed that DCI contents steadily increased at early stage of germination and reached the highest level of 33.42 μg/seed at 24 h during the 72 h trail. However, the total fagopyritol contents sharply decreased from 214.6 μg/seed to 46 μg/seed at the end of the germination. The activity of acid α-galactosidase increased gradually to the peak of 0.36 nkat/seed at 24 h after the primed seed imbibition. We cloned the gene fragment of α-galactosidase in tartary buckwheat for the first time. The deduced amino acid sequence is 93% identical to that of P. vulgaris. The quantitative PCR result of gene expression pattern was consistent with its enzyme activity during seed germination.
11

Effect of dehulling and alpha-galactosidase supplement on the ileal digestibility of yellow lupin based diets in broiler chickens and adult roosters

51%
Mieczkowska A., Jansman A. J. M., Kwakkel R. P., Smulikowska S.
Journal of Animal and Feed Sciences
|
2005
|
tom 14
|
nr 2
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