Submit Manuscript

Pakistan Journal of Biological Sciences

Year: 2015 | Volume: 18 | Issue: 6 | Page No.: 279-284
Facebook Twitter Digg Reddit Linkedin StumbleUpon E-mail

Article Trend

Total views 178

Authors

Berna Elya

Rosita Handayani

Rani Sauriasari

Azizahwati

Uqie Shabrina Hasyyati

Idam Titis Permana

Yunita Indah Permatasari

Keywords

Active compounds of plants have potency as antidiabetic that can be used in diabetes mellitus treatment. One of the strategies is maintaining postprandial glucose level through inhibition of α-amylase and α-glucosidase and preventing the hydrolysis of Glucagon Like Peptide-1 (GLP-1) through inhibition of Dipeptidyl peptidase IV. So that pre-prandial and post-prandial glucose levels can be controlled properly. The aim of this study was to determine in vitro inhibitory activity of α-glucosidase, α-amylase and Dipeptidyl peptidase IV from 42 ethanolic extracts of selected Indonesian plants. Inhibitory activity was measured using spectrophotometric method. α-amylase activity was measured at λ = 540 nm, α-glucosidase activity and the DPP-IV activity were measured at λ = 405 nm. Eight extracts inhibit both α-glucosidase and α-amylase better than acarbose as a positive control. These extracts are Camelia sinensis (white, green, fermented), Pometia pinnata, Syzygium polyanthum, Artocarpus heteropyllus, Lagerstroemia speciosa and Persea Americana. The ethanolic extracts have DPP-IV inhibitory activity between 10-20%, lower than Diprotin as positive control, except Camelia sinensis (white) which gave the inhibition more than 30% at 62.5 μg mL–1. This study showed us that some extracts have inhibition activity of α-glucosidase, α-amylase and DPP-IV.
PDF Fulltext XML References Citation

How to cite this article

Berna Elya, Rosita Handayani, Rani Sauriasari, Azizahwati, Uqie Shabrina Hasyyati, Idam Titis Permana and Yunita Indah Permatasari, 2015. Antidiabetic Activity and Phytochemical Screening of Extracts from Indonesian Plants by Inhibition of Alpha Amylase, Alpha Glucosidase and Dipeptidyl Peptidase IV. Pakistan Journal of Biological Sciences, 18: 279-284.

DOI: 10.3923/pjbs.2015.279.284

URL: https://scialert.net/abstract/?doi=pjbs.2015.279.284

Leave a Comment

Your email address will not be published. Required fields are marked *