Traditional Processing of Arum maculatum L. and Apparent α-Amylase Inhibition: An Exploratory In Vitro and In Silico Study
5 affiliations
- 1Department of Analytical Chemistry, Hamidiye Faculty of Pharmacy, University of Health Sciences Türkiye, 34668 İstanbul, Türkiye
- 2Hamidiye Faculty of Pharmacy, University of Health Sciences Türkiye, 34668 İstanbul, Türkiye
- 3Department of Bioengineering, Faculty of Chemical and Metallurgical Engineering, Yildiz Technical University, 34220 İstanbul, Türkiye
- 4Department of Biochemistry, Hamidiye Faculty of Pharmacy, University of Health Sciences Türkiye, 34668 İstanbul, Türkiye
- 5Department of Pharmacognosy, Faculty of Pharmacy, Altınbaş University, Bakırköy Health Campus, 34145 İstanbul, Türkiye
Abstract
Arum maculatum L. is a traditionally consumed but toxic and irritant plant that must be processed before use. This exploratory study examined whether three preparations—an ethanol:water (80:20, v/v) extract of dried material (E1), a corresponding extract of fresh material (E2) and an aqueous decoction of fresh material (E3) mirroring traditional boiling—differ in apparent α-amylase inhibition, and whether their previously reported phenolic marker profiles (high-performance liquid chromatography with photodiode array detection, HPLC–PDA) account for these differences. Inhibition of Aspergillus oryzae α-amylase was measured by the starch–iodine method at a single extract concentration and two enzyme loadings, using one extract per preparation and analytical triplicates. All extracts gave higher apparent inhibition values (75.13–90.80%) than the assay-internal acarbose control (67.28–68.15%) at the same nominal mass concentration (40 µg/mL), with E3 highest at the higher enzyme loading. The previously quantified markers did not account for this pattern. Docking against fungal (3VX0, 7TAA) and human (2QV4, 4GQR) α-amylases placed all markers in the catalytic cleft, a hypothesis-generating result that does not establish binding affinity. These descriptive differences indicate that processing is associated with different apparent α-amylase inhibition, whereas the active constituents, possible assay interference and the safety of the preparations remain to be established.
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BibTeX
@article{ozdemir2026traditional,
title = {{Traditional Processing of Arum maculatum L. and Apparent α-Amylase Inhibition: An Exploratory In Vitro and In Silico Study}},
author = {Zafer Ömer Özdemir and Ezgi Keskin and Mustafa Niğde and Duygu Mısırlı and Ebru Özdemir Nath and Mahfuz Elmastaş},
journal = {Molecules},
year = {2026},
month = nov,
doi = {10.3390/molecules31213994},
url = {https://www.mdpi.com/1420-3049/31/21/3994},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Traditional Processing of Arum maculatum L. and Apparent α-Amylase Inhibition: An Exploratory In Vitro and In Silico Study
AU - Zafer Ömer Özdemir
AU - Ezgi Keskin
AU - Mustafa Niğde
AU - Duygu Mısırlı
AU - Ebru Özdemir Nath
AU - Mahfuz Elmastaş
PY - 2026
DA - 2026/11/05
JO - Molecules
DO - 10.3390/molecules31213994
UR - https://www.mdpi.com/1420-3049/31/21/3994
AB - Arum maculatum L. is a traditionally consumed but toxic and irritant plant that must be processed before use. This exploratory study examined whether three preparations—an ethanol:water (80:20, v/v) extract of dried material (E1), a corresponding extract of fresh material (E2) and an aqueous decoction of fresh material (E3) mirroring traditional boiling—differ in apparent α-amylase inhibition, and whether their previously reported phenolic marker profiles (high-performance liquid chromatography with photodiode array detection, HPLC–PDA) account for these differences. Inhibition of Aspergillus oryzae α-amylase was measured by the starch–iodine method at a single extract concentration and two enzyme loadings, using one extract per preparation and analytical triplicates. All extracts gave higher apparent inhibition values (75.13–90.80%) than the assay-internal acarbose control (67.28–68.15%) at the same nominal mass concentration (40 µg/mL), with E3 highest at the higher enzyme loading. The previously quantified markers did not account for this pattern. Docking against fungal (3VX0, 7TAA) and human (2QV4, 4GQR) α-amylases placed all markers in the catalytic cleft, a hypothesis-generating result that does not establish binding affinity. These descriptive differences indicate that processing is associated with different apparent α-amylase inhibition, whereas the active constituents, possible assay interference and the safety of the preparations remain to be established.
SN - 1420-3049
ER -