Comparative physico-kinetic properties of a homogenous purified β-glucosidase from Withania somnifera leaf

Mishra, Siddhartha; Sangwan, Neelam S.; Sangwan, Rajender S.

doi:10.1007/s11738-012-1183-8

Cited by 7 publications

(1 citation statement)

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“…We have recently established methods for the purification and characterization of enzymes involved in the glycosylation of natural products from medicinal plants such as Withania somnifera (Mishra et al , 2013a) and Andrographis paniculata (Mishra et al , 2013b). A β-glucosidase was purified from the petals of S. marianum using the ammonium sulphate precipitation method, followed by enrichment using Sephacryl-200, Q-Sepharose and S-Sepharose (Mishra et al , 2013c).…”

Section: Methodsmentioning

confidence: 99%

Proteomic identification of a fucosyltransferase from petals of milk thistle, Silybum marianum

Mishra

Sangwan

Srivastava

et al. 2014

Plant Genet. Resour.

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Fucosyltransferases are a group of enzymes that catalyse the transfer of L-fucose from a donor substrate to an acceptor molecule. Silybum marianum is also called 'milk thistle' due to its characteristic flower shape. It produces two major flavonoids: silymarin and silybin. The plant and its major secondary metabolites are used for treatment/recovery after chronic liver disease, liver rehabilitation after hepatitis and treatment of gallbladder disease. These compounds also act as antioxidants for scavenging free radicals and inhibiting lipid peroxidation. We identified two peptide motifs (YYEAYLSHADEK and TTPDPSCGR designated as motif 1 and motif 2, respectively) of a fucosyltransferase derived from S. marianum that are highly conserved in its counterparts across the plant species and sources. The nature and properties of the motifs are discussed in terms of their putative participation in catalysis and enzyme/active site conformation.

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Section: Methodsmentioning

confidence: 99%