Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylase
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 interac...
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| Format: | Article |
| Language: | English |
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Elsevier
2022-12-01
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| Series: | Ecotoxicology and Environmental Safety |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S0147651322010661 |
| _version_ | 1798017252250877952 |
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| author | Ananthaselvam Azhagesan Natarajan Chandrasekaran Amitava Mukherjee |
| author_facet | Ananthaselvam Azhagesan Natarajan Chandrasekaran Amitava Mukherjee |
| author_sort | Ananthaselvam Azhagesan |
| collection | DOAJ |
| description | 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 (Ka) was 1.904 × 1019 M-1. S-1 while the quenching constant (Kq) was 1.036 × 1011 M-1, the blue shift of the peak showed static quenching. The binding constant was KA = 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 IC50 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. |
| first_indexed | 2024-04-11T16:04:04Z |
| format | Article |
| id | doaj.art-bb3e5b52708b48d587ffd974aafa48f4 |
| institution | Directory Open Access Journal |
| issn | 0147-6513 |
| language | English |
| last_indexed | 2024-04-11T16:04:04Z |
| publishDate | 2022-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Ecotoxicology and Environmental Safety |
| spelling | doaj.art-bb3e5b52708b48d587ffd974aafa48f42022-12-22T04:14:52ZengElsevierEcotoxicology and Environmental Safety0147-65132022-12-01247114226Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylaseAnanthaselvam Azhagesan0Natarajan Chandrasekaran1Amitava Mukherjee2Centre for Nanobiotechnology, Vellore Institute of Technology (VIT), Vellore 632 014, Tamil Nadu, IndiaCorresponding author.; Centre for Nanobiotechnology, Vellore Institute of Technology (VIT), Vellore 632 014, Tamil Nadu, IndiaCentre for Nanobiotechnology, Vellore Institute of Technology (VIT), Vellore 632 014, Tamil Nadu, IndiaThe 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 (Ka) was 1.904 × 1019 M-1. S-1 while the quenching constant (Kq) was 1.036 × 1011 M-1, the blue shift of the peak showed static quenching. The binding constant was KA = 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 IC50 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.http://www.sciencedirect.com/science/article/pii/S0147651322010661α-AmylaseEnzymes InhibitionFluorescence quenchingKineticsAnd Nano polystyrene |
| spellingShingle | Ananthaselvam Azhagesan Natarajan Chandrasekaran Amitava Mukherjee Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylase Ecotoxicology and Environmental Safety α-Amylase Enzymes Inhibition Fluorescence quenching Kinetics And Nano polystyrene |
| title | Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylase |
| title_full | Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylase |
| title_fullStr | Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylase |
| title_full_unstemmed | Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylase |
| title_short | Multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α-amylase |
| title_sort | multispectroscopy analysis of polystyrene nanoplastic interaction with diastase α amylase |
| topic | α-Amylase Enzymes Inhibition Fluorescence quenching Kinetics And Nano polystyrene |
| url | http://www.sciencedirect.com/science/article/pii/S0147651322010661 |
| work_keys_str_mv | AT ananthaselvamazhagesan multispectroscopyanalysisofpolystyrenenanoplasticinteractionwithdiastaseaamylase AT natarajanchandrasekaran multispectroscopyanalysisofpolystyrenenanoplasticinteractionwithdiastaseaamylase AT amitavamukherjee multispectroscopyanalysisofpolystyrenenanoplasticinteractionwithdiastaseaamylase |