2011
DOI: 10.1590/s1677-04202011000100003
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Abstract: Three β-galactosidase isoforms, β-gal I and β-gal II (cytosolic) and β-gal III (cell wall-associated), were isolated from stems of Vigna unguiculata (L.) Walp. cv. Pitiúba seedlings. Purification consisted of ammonia sulfate fractionation followed by chromatography in DEAE-Sephadex and Lactosyl-Sepharose columns. The two cytosolic isoforms showed the same chromatography pattern, which differed from that of β-gal III. Electrophoresis revealed a single band of protein for β-gal II and β-gal III which also expres… Show more

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Cited by 4 publications
(39 citation statements)
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References 26 publications
(39 reference statements)
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“…In a similar way to the results found here, several studies with -galactosidases purified from plants showed that isoforms of these enzymes present F. B. Sudério et al diverse molecular weights (ALCÂNTARA et al, 2006;BALASUBRAMANIAM et al, 2005;BISWAS;KAYASTHA;SECKLER, 2003;SUDÉRIO et al, 2011b). The activities of the cytosolic -galactosidases ( -gal I and II) and cell wall -galactosidase ( -gal III) as a function of the pH of the reaction medium, showed an increase from pH 2.5 until reaching maximum activity at pH 4.0, with a progressive decrease to pH 6.5 (Figure 1).…”
Section: Resultssupporting
confidence: 88%
“…The optimum test temperature for the -gal I, II and III enzymes was 55 °C, with a considerable drop in activity from 60 °C. The range seen for the optimum test temperature is similar to those found for other -galactosidases purified from plants (CHILAKA;OKEKE;ADAIKPOH, 2002;ENÉAS-FILHO et al, 2000;ENÉAS-FILHO, 2001;SUDÉRIO et al, 2011b). In the study of thermostability, -gal I showed a reduction in activity when incubated at just 40 °C, with all enzymes showing a sharp drop in activity at 60 °C until complete inactivation at 70 °C (Figure 2).…”
Section: Resultssupporting
confidence: 72%
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“…β-galactosidases have been detected in a wide range of plant organs and tissues and are described by their ability to hydrolyze terminal non-reducing β-D-galactosyl residues from β-D-galactosides [16]. It has been purified from various plant sources, like chick pea [17], almond [6], apricots [18], Vigna unguiculata [19], apricot seed [20]. β-galactosidase play key roles in fruit ripening.…”
Section: Introductionmentioning
confidence: 99%
“…Many studies have indicated remarkable increase in expression level of mRNA β-galactosidase during fruit ripening in many fruits [24,25]. It was reported that β-galactosidases are widely distributed in many plant tissues, like seeds [6,20], stems [19], and meristem zones of roots, trichomes, cotyledons, vascular tissues, and pollens [26,27]. On the other hand, it also participates in the cell wall modification during elongation and differentiation of plant cells [28,29].…”
Section: Introductionmentioning
confidence: 99%