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Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylase
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Researchers used fluorescence spectroscopy and other analytical techniques to characterize how polystyrene nanoplastics bind to and alter the structure of alpha-amylase, a key digestive enzyme, suggesting nanoplastic exposure could potentially disrupt starch digestion.
The digestive enzyme of plant are generally α-amylase. They functions enzyme that breakdown starch into maltose and sugars. This happens in the endosperm of the seed. Due to pollutants, this process get happened one of emergent xenobiotics are micro and nano plastics. This study involves the interaction 100 nm size of polystyrene nano plastic (PSNPs) on α-amylase. The hyperchromism of α-amylase - PSNPs conjugate's revealed that ground-state complex in a microenvironment. Fluorescence quenching happened when the concentration of PSNPs was increased. The Stern Volmer plot revealed binding constant (K) was 1.904 × 1019 M. S while the quenching constant (K) was 1.036 × 1011 M, the blue shift of the peak showed static quenching. The binding constant was K = 4.2 × 1012, the number of binding site on PSNPs for α-amylase was n = 1.12. The synchronous result showed a gradual reduction in the intensity of Trp residues because when the α-amylase interacts with PSNPs short-range π-π interaction happens around the Trp163 residues. The enzyme activity of α-amylase by 44 % and its IC value was found to be 100 µg/mL. The enzyme kinetics (Vmax) analysis showed the type of inhibition with and without PSNPs Vmax 769 and Vmax 303 µg/mL/min, uncompetitive inhibition respectively. The effect of PSNPs on the enzymatic activity of α-amylase showed structural alterations of the protein. Therefore the in vitro and in silico studies were shown evidence of interaction between α-amylase and PSNPs leads to conformational structural changes in α-amylase.
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