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Journal ArticleDOI

Multiple forms of β-galactosidase from the germinating seeds of Vigna radiata

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TLDR
Four forms of β-galactosidase were isolated and partially purified from the cotyledons of germinating seeds of Vigna radiata by ammonium sulphate fractionation and ion exchange chromatography through DEAE-cellulose and CM- cellulose columns, showing similar pH optima and temperature optima but differed from each other in ionic charge, kinetic parameters, activation energy and sensitivity towards heat.
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This article is published in Phytochemistry.The article was published on 1990-01-01. It has received 11 citations till now. The article focuses on the topics: Galactoside.

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Journal ArticleDOI

Kiwifruit β-galactosidase: Isolation and activity against specific fruit cell-wall polysaccharides

TL;DR: Results indicate that the β-galactosidase of this study is solely responsible for the removal of galactose from the cell wall during ripening, and its in-vivo activity must be much greater than that observed in- vitro.
Journal ArticleDOI

Purification and properties of a novel beta-galactosidase or exo-(1-->4)-beta-D-galactanase from the cotyledons of germinated Lupinus angustifolius L. seeds.

TL;DR: The exo-galactanase is clearly a key enzyme in galactan mobilisation and may be the sole activity involved in depolymerising the dominant (1 → 4)-β-Galactan component of the cell wall.
Journal ArticleDOI

Purification and characterization of isoforms of β-galactosidases in mung bean seedlings

TL;DR: Double immunodiffusion analysis indicated thatbeta-galactosidases I, II, III and V are immunologically similar to each other, while beta-galactsosidase IV shares partially identical antigenic determinants with the other four isoforms.
Journal ArticleDOI

Xyloglucan mobilisation and purification of a (XLLG/XLXG) specific β-galactosidase from cotyledons of Copaifera langsdorffii

TL;DR: The β-galactosidase isolated from cotyledons of germinating seeds of Copaifera langsdorffii seems to perform a key role in xyloglucan degradation since it is responsible for the retrieval of a major sterical hindrance for further hydrolysis of the oligosaccharides and therefore essential for completion of xylglucan mobilisation.
Journal ArticleDOI

β-Galactosidase from Coffea Arabica and its role in fruit ripening

TL;DR: β -Galactosidase activity in coffee berries showed a progressive increase of more than four-fold as the fruit developed from the immature to ripe stage, with a slight decrease in fully ripe fruit, suggesting that β-galactsidase plays a role in cell wall degradation such as occurs during fruit ripening.
References
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Journal ArticleDOI

Isolation and characterization of jack bean beta-galactosidase.

TL;DR: Results suggest that in addition to the type and linkage of the penultimate sugar unit, the sugar unit at the distal position of the saccharide chain also affects the hydrolysis rate of beta-galactosidase.
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Gm1 Ganglioside β-Galactosidase A PURIFICATION AND STUDIES OF THE ENZYME FROM HUMAN LIVER

TL;DR: Gm1-ganglioside β-galactosidase A (EC 3.2.1.23) has been purified 17,000-fold from human liver and appeared as a single band of protein on polyacrylamide gel electrophoresis.
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Characteristics of β‐galactosidase purified from cell suspension cultures of carrot

TL;DR: The glycosidase was slightly involved in the hydrolysis of the pectic polymer and cell walls purified from carrot cell cultures and acted on the β-1,4-linked galactan prepared from citrus pectin in an exo-fashion.
Journal ArticleDOI

β-Galactosidases of Lilium pollen

TL;DR: The total β-galactosidase activity of lily pollen remained constant during in vitro germination, suggesting a possible role for this enzyme may be in degradation of stylar arabinogalactans providing a carbon source for pollen tube nutrition.
Journal ArticleDOI

Occurrence of glycoprotein glycosidases in mature seeds of mung bean (vigna radiata)

TL;DR: With the exception of β-galactosidase and invertase, all the glycosidase activities were detected in the protein bodies isolated from the seeds, indicating differences in glycosylation.
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