Purification of α-galactosidase from coconut

Balasubramaniam, K.; Mathew, C. Deepal

doi:10.1016/s0031-9422(00)81155-3

Cited by 10 publications

(4 citation statements)

References 16 publications

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“…This fraction eluted in the zone corresponding to 120-140 kDa. Similar molecular weights have been described for an a-galaetosidase from coconut endosperm (120 kDa) (Balasubramaniam and Mathew 1986). In our work, the a-galactosidase was purified 6-fold (Tab.…”

Section: Partial Purification Of the Fraction With A-galactosidase Acsupporting

confidence: 71%

Partial purification of cell wall α‐galactosidases and α‐arabinosidases from Cicer arietinum epicotyls. Relationship with cell wall autolytic processes

Dopico

Nicolás

Labrador

1989

Physiologia Plantarum

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Two protein fractions with activity as α‐galactosidase (EC 3.2.1.22) and α‐arabinosidase (EC 3.2.1.55), respectively, were identified in the proteins of cell wall of Cicer arietinum L. cv. Castellana extracted with 3 M LiCl. These fractions were partially purified by gel filtration chromatography (Bio Gel P‐150), increasing the specific arabinosidase activity 57‐fold and the α‐galactosidase activity 6‐fold. Other protein fractions with glucosidase (EC 3.2.1.21) and glucanase (EC 3.2.1.6) activity also appeared. According to earlier authors, α‐arabinosidases and α‐galactosidases are related to alterations in linkages occurring in cell walls, since the enzymes are able to hydrolyze isolated wall polymers. However, our preparations hydrolyze intact cell walls only to a very limited extent, such that their participation in the autolytic processes of cell walls can be ruled out.

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Section: Partial Purification Of the Fraction With A-galactosidase Acsupporting

confidence: 71%

Partial purification of cell wall α‐galactosidases and α‐arabinosidases from Cicer arietinum epicotyls. Relationship with cell wall autolytic processes

Dopico

Nicolás

Labrador

1989

Physiologia Plantarum

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“…Alpha-galactosidase has been isolated from various sources such as plant seeds (Dey and Pridham 1969;Williams et al 1977) and coconut (Balasubramaniam and Mathew 1986). For some unknown reasons, most of them have difficulty in cleaving the terminal α1→4 linked galactose in sphingoglycolipids.…”

Section: Introductionmentioning

confidence: 99%

Cloning, Expression, and Characterization of Rice α-Galactosidase

2008

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We have successfully cloned an α-galactosidase gene from a rice cDNA library and transformed it into Escherichia coli BL21. It was subsequently cloned to the pPIC9K vector and expressed in Pichia pastoris. A selected clone was found to result in high production yield of the galactosidase enzyme. The secreted enzyme was purified, and it revealed as a major protein band on an SDS-PAGE gel. The optimal pH value, enzyme stabilities, and substrate specificity were studied. The enzyme specificity toward the terminal α1→6, 1→4, and 1→3 linked galactosyl residue from various substrates was investigated. By determining the Michelis constant (Km) of the enzyme for melibiose, raffinose, and stachyose, our results showed that melibiose was hydrolyzed faster than raffinose, whereas the published data reported a reversed sequence, raffinose > melibiose. The enzyme also showed the ability of converting B red blood cells into O red cells. The objective of this work is to develop the Pichia system to produce a large quantity of enzyme for blood cell conversion for transfusion.

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“…The enzyme is found in legume seeds and other vegetable sources (Balasubramaniam & Mathew, 1986;Bayraktar & Onal, 2013;Bryant & Rao, 2000;Chinen et al, 1981;Feurtado et al, 2001;Kang & Lee, 2001;Kim et al, 2002Kim et al, , 2003Malhotra & Dey, 1967;Marraccini et al, 2005;Zhifang & Schaffer, 1999). It is present in sweet almond (Malhotra & Dey, 1967), melon fruit (Zhifang & Schaffer, 1999) endosperm of coconut (Balasubramaniam & Mathew, 1986) and sunflower seeds (Kim et al, 2003). Two alkaline and one acid α-D-galactosidases were identified in melon fruit, including a novel alkaline form with activity toward a broader spectrum of galactosyl saccharides, particularly raffinose.…”

Section: Sources Of α-D-galactosidasesmentioning

confidence: 99%

Hooked on α-d-galactosidases: from biomedicine to enzymatic synthesis

Bakunina

Balabanova

Pennacchio

et al. 2015

Critical Reviews in Biotechnology

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α-d-Galactosidases (EC 3.2.1.22) are enzymes employed in a number of useful bio-based applications. We have depicted a comprehensive general survey of α-d-galactosidases from different origin with special emphasis on marine example(s). The structures of natural α-galactosyl containing compounds are described. In addition to 3D structures and mechanisms of action of α-d-galactosidases, different sources, natural function and genetic regulation are also covered. Finally, hydrolytic and synthetic exploitations as free or immobilized biocatalysts are reviewed. Interest in the synthetic aspects during the next years is anticipated for access to important small molecules by green technology with an emphasis on alternative selectivity of this class of enzymes from different sources.

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Purification of α-galactosidase from coconut

Cited by 10 publications

References 16 publications

Partial purification of cell wall α‐galactosidases and α‐arabinosidases from Cicer arietinum epicotyls. Relationship with cell wall autolytic processes

Partial purification of cell wall α‐galactosidases and α‐arabinosidases from Cicer arietinum epicotyls. Relationship with cell wall autolytic processes

Cloning, Expression, and Characterization of Rice α-Galactosidase

Hooked on α-d-galactosidases: from biomedicine to enzymatic synthesis

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