Purification and Biochemical Characterization of α-Amylase from Radish (Raphanus sativus L.) Seeds Using Response surface methodology

Khare, Saumya; Prakash, Om

doi:10.1007/s40011-017-0921-5

Cited by 5 publications

(1 citation statement)

References 24 publications

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“…The activity of α-amylase was carried out using starch as a substrate as described by Khare and Prakash 34 . Reaction mixture (1.0 ml) containing starch was dissolved in sodium phosphate buffer (100 mM, pH 6.9), suitably diluted porcine pancreatic α-amylase was incubated at 27 °C for 3 min.…”

Section: Methodsmentioning

confidence: 99%

Characterization and evaluation of mycosterol secreted from endophytic strain of Gymnema sylvestre for inhibition of α-glucosidase activity

Ranjan

Singh

Khare

et al. 2019

Sci Rep

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Endophytic fungi produce various types of chemicals for establishment of niche within the host plant. Due to symbiotic association, they secrete pharmaceutically important bioactive compounds and enzyme inhibitors. In this research article, we have explored the potent α-glucosidse inhibitor (AGI) produced from Fusarium equiseti recovered from the leaf of Gymnema sylvestre through bioassay-guided fraction. This study investigated the biodiversity, phylogeny, antioxidant activity and α-glucosidse inhibition of endophytic fungi isolated from Gymnema sylvestre. A total of 32 isolates obtained were grouped into 16 genera, according to their morphology of colony and spores. A high biodiversity of endophytic fungi were observed in G. sylvestre with diversity indices. Endophytic fungal strain Fusarium equiseti was identified through DNA sequencing and the sequence was deposited in GenBank database (https://ncbi.nim.nih.gov) with acession number: MF403109. The characterization of potent compound was done by FTIR, LC-ESI-MS and NMR spectroscopic analysis with IUPAC name 17-(5-ethyl-6-methylheptan-2-yl)-10,13-dimethyl-2,3,4,7,8,9,10,11,12,13,14,15,16,17-tetradecahydro-1H-cyclopenta[a] phenanthren-3-ol. The isolated bioactive compound showed significant α-amylase and α-glucosidase inhibition activity with IC50 values, 4.22 ± 0.0005 µg/mL and 69.72 ± 0.001 µg/mL while IC50 values of acarbose was 5.75 ± 0.007 and 55.29 ± 0.0005 µg/mL respectively. This result is higher in comparison to other previous study. The enzyme kinetics study revealed that bioactive compound was competitive inhibitor for α-amylase and α-glucosidase. In-silico study showed that bioactive compound binds to the binding site of α-amylase, similar to that of acarbose but with higher affinity. The study highlights the importance of endophytic fungi as an alternative source of AGI (α-glucosidase inhibition) to control the diabetic condition in vitro.

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Section: Methodsmentioning

confidence: 99%