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. 1967 May;103(2):508–513. doi: 10.1042/bj1030508

Purification and physical properties of sweet-almond α-galactosidase

O P Malhotra 1,*, Prakash Mohan Dey 1,†
PMCID: PMC1270435  PMID: 6032983

Abstract

1. α-Galactosidase from sweet almonds was purified about 2000-fold through eight steps. 2. The enzyme preparation was free from other related enzymes known to occur in sweet almonds, and behaved as a homogeneous protein on filtration through Sephadex G-75. 3. A molecular weight of about 33000 was determined from the gel-filtration data. 4. The ultraviolet-absorption spectrum and thermal inactivation of the enzyme are described. 5. The purified enzyme hydrolysed p-nitrophenyl α-d-galactoside at a much faster rate than melibiose. 6. The pH optimum was at 5·5–5·7. 7. Besides hydrolysis, it also catalysed transfer of galactosyl residues, chain elongation of melibiose and the synthesis of oligosaccharides from galactose.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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