ArticleHeliyon2025
Responses of α-amylase and protease activity to chemical agents and metallic salts in barley seeds (
Article in Heliyon, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Highly efficient degradation of polybutylene succinate (PBS) and polycaprolactone (PCL) by a recombinant marine fungal cutinase.Applied and environmental microbiology · 2025Article
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
In modern agriculture, the enzymes inhibition by chemical agents and environmental pollutants accounts for a significant threat to crop health and productivity. Enzymes play a crucial role in maintaining homeostasis in the metabolic processes that sustain life. Understanding what regulates enzyme activity is crucial for many scientific and industrial endeavors. The purpose of this research work was to examine how different chemical agents, and metallic salts affected the activity of two important food enzymes like α-amylase and protease in barley. These studies compared the effects of several chemical treatments applied to barley seeds, including urea, ethylenediaminetetraacetic acid (EDTA), acetic acid, and a wide range of metallic salts. To determine the impact of each chemical on the stability of α-amylase and protease enzyme activity using standard assay procedures. The activities of α-amylase and protease were inhibited by increasing urea concentration, eventually eliminating them at 8 M urea. The enzymes lost their activities completely at 0.50 M EDTA. Treatment with higher acetic acid concentrations decreased their activities, but they retained 20.46 ± 1.06 % and 17.38 ± 1.09 % after treating with 20 % acetic acid. The application of CaCl
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Registered trials
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