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Updated: Aug 5, 2026
10:58
Plant Promoter Analysis: Identification and Characterization of Root Nodule Specific Promoter in the Common Bean
Published on: December 23, 2017
Summary
Fababean seed extract binds zinc (Zn2+), primarily through phytate. Removing phytate with the enzyme phytase significantly reduced this zinc binding capacity.
Area of Science:
- Agricultural Chemistry
- Food Science
- Nutritional Biochemistry
Background:
- Phytate is a major storage form of phosphorus in plant seeds.
- Phytate can chelate essential minerals, including zinc, potentially affecting their bioavailability.
- Fababeans are a significant legume crop with potential nutritional contributions.
Purpose of the Study:
- To investigate the role of phytate in zinc (Zn2+) binding within an aqueous fababean extract.
- To quantify the effect of phytase treatment on zinc binding by the fababean extract.
Main Methods:
- Spectrophotometric analysis was used to estimate Zn2+ binding.
- Treatment with the enzyme phytase was employed to remove phytate.
- Gel permeation chromatography was utilized to characterize the Zn2+ binding components.
Main Results:
- The aqueous fababean extract demonstrated significant binding of Zn2+.
- Treatment with phytase removed nearly all phytate and approximately 82% of the Zn2+ binding capacity.
- Chromatographic analysis indicated that phytate co-eluted with the primary Zn2+ binding factor.
Conclusions:
- Phytate is identified as the major constituent responsible for Zn2+ binding in the fababean extract.
- The findings highlight the impact of phytate on zinc bioavailability from fababeans.
- Enzymatic removal of phytate offers a potential strategy to enhance zinc absorption from fababean-based foods.
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