The Binding Affinity of Small Molecules with Yam Tyrosinase (Catechol Oxidase): A Biophysical Study

Yam tyrosinase has become an economically essential enzyme due to its ease of purification and abundant availability of yam tubers. However, an efficient biochemical and biophysical characterization of yam tyrosinase has not been reported. In the present study, the interaction of yam (Amorphophallus...

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Main Authors: Tabassum Mulla, Sushama Patil, Srinivas Sistla, Jyoti Jadhav
Format: Article
Language:English
Published: Wiley 2019-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2019/8284968
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author Tabassum Mulla
Sushama Patil
Srinivas Sistla
Jyoti Jadhav
author_facet Tabassum Mulla
Sushama Patil
Srinivas Sistla
Jyoti Jadhav
author_sort Tabassum Mulla
collection DOAJ
description Yam tyrosinase has become an economically essential enzyme due to its ease of purification and abundant availability of yam tubers. However, an efficient biochemical and biophysical characterization of yam tyrosinase has not been reported. In the present study, the interaction of yam (Amorphophallus paeoniifolius) tyrosinase was studied with molecules such as crocin (Crocus sativus), hydroquinone, and kojic acid. Surface plasmon resonance (SPR), fluorescence spectroscopy, and circular dichroism techniques were employed to determine the binding affinities and the changes in secondary and tertiary structures of yam tyrosinase in the presence of four relevant small molecules. Hydroquinone and crocin exhibited very low binding affinities of 0.24 M and 0.0017 M. Due to their apparent weak interactions, competition experiments were used to determine more precisely the binding affinities. Structure-function interrelationships can be correlated in great detail by this study, and the results can be compared with other available tyrosinases.
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institution Kabale University
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series Biochemistry Research International
spelling doaj-art-15031b4290544f32b3b275ae9c8f60272025-02-03T06:12:23ZengWileyBiochemistry Research International2090-22472090-22552019-01-01201910.1155/2019/82849688284968The Binding Affinity of Small Molecules with Yam Tyrosinase (Catechol Oxidase): A Biophysical StudyTabassum Mulla0Sushama Patil1Srinivas Sistla2Jyoti Jadhav3Department of Biotechnology, Shivaji University, Kolhapur 416004, IndiaDepartment of Biotechnology, Shivaji University, Kolhapur 416004, IndiaInstitute for Structural Biology, Drug Discovery and Development, Virginia Commonwealth University, Richmond, VA 23298, USADepartment of Biotechnology, Shivaji University, Kolhapur 416004, IndiaYam tyrosinase has become an economically essential enzyme due to its ease of purification and abundant availability of yam tubers. However, an efficient biochemical and biophysical characterization of yam tyrosinase has not been reported. In the present study, the interaction of yam (Amorphophallus paeoniifolius) tyrosinase was studied with molecules such as crocin (Crocus sativus), hydroquinone, and kojic acid. Surface plasmon resonance (SPR), fluorescence spectroscopy, and circular dichroism techniques were employed to determine the binding affinities and the changes in secondary and tertiary structures of yam tyrosinase in the presence of four relevant small molecules. Hydroquinone and crocin exhibited very low binding affinities of 0.24 M and 0.0017 M. Due to their apparent weak interactions, competition experiments were used to determine more precisely the binding affinities. Structure-function interrelationships can be correlated in great detail by this study, and the results can be compared with other available tyrosinases.http://dx.doi.org/10.1155/2019/8284968
spellingShingle Tabassum Mulla
Sushama Patil
Srinivas Sistla
Jyoti Jadhav
The Binding Affinity of Small Molecules with Yam Tyrosinase (Catechol Oxidase): A Biophysical Study
Biochemistry Research International
title The Binding Affinity of Small Molecules with Yam Tyrosinase (Catechol Oxidase): A Biophysical Study
title_full The Binding Affinity of Small Molecules with Yam Tyrosinase (Catechol Oxidase): A Biophysical Study
title_fullStr The Binding Affinity of Small Molecules with Yam Tyrosinase (Catechol Oxidase): A Biophysical Study
title_full_unstemmed The Binding Affinity of Small Molecules with Yam Tyrosinase (Catechol Oxidase): A Biophysical Study
title_short The Binding Affinity of Small Molecules with Yam Tyrosinase (Catechol Oxidase): A Biophysical Study
title_sort binding affinity of small molecules with yam tyrosinase catechol oxidase a biophysical study
url http://dx.doi.org/10.1155/2019/8284968
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