Temperature-Dependent Structure–Function Properties of Bacterial Xylose Isomerase Enzyme for Food Applications: An In Silico Study
Xylose Isomerase (XI) is an intramolecular oxidoreductase enzyme and catalyzes the reversible conversion of ketoses and aldoses in addition to the bioconversion of ethanol from xylose in the production of bioethanol from hemicellulose. It has a broad range of industrial applications in the food and...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-12-01
|
| Series: | Clean Technologies |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2571-8797/4/4/81 |
| _version_ | 1797460841616900096 |
|---|---|
| author | Maurya Sharma Naayaa Mehta Renuka Suravajhala Cynthia Meza Shrabana Sarkar Aparna Banerjee |
| author_facet | Maurya Sharma Naayaa Mehta Renuka Suravajhala Cynthia Meza Shrabana Sarkar Aparna Banerjee |
| author_sort | Maurya Sharma |
| collection | DOAJ |
| description | Xylose Isomerase (XI) is an intramolecular oxidoreductase enzyme and catalyzes the reversible conversion of ketoses and aldoses in addition to the bioconversion of ethanol from xylose in the production of bioethanol from hemicellulose. It has a broad range of industrial applications in the food and pharmaceutical sectors, particularly in the production of the sweetener high fructose corn syrup (HFCS). It is one of the most widely used industrial enzymes after protease. Taking this into consideration, four bacterial XI sources were selected based on growth temperature, i.e., psychrophile, mesophile, thermophile, and hyperthermophile, for analyzing Xylose Isomerase’s structure-function characteristics. It was found that thermophilic XI was structurally less stable than mesophilic and hyperthermophilic XI, whereas structural plasticity ran opposite towards mesophiles. The interaction of xylose isomerase (XI) with two ligands, namely Amino-2-Hydroxymethyl-Propane-1,3-Diol and (4R)-2-Methylpentane-2,4- Diol, was also studied. Mesophilic XI demonstrated better binding affinity with structurally stabilizing amino acids (Ala, Asp, Gly, Leu, and Arg). In comparison, Thermophilic XI showed nearly similar binding affinity with both Amino-2-Hydroxymethyl-Propane-1,3-Diol and (4R)-2-Methylpentane-2,4-Diol. The results of this investigation suggest that thermophilic XI, followed by mesophilic XI, would be the most appropriate for establishing process stability and sustainability in the food industry. |
| first_indexed | 2024-03-09T17:10:49Z |
| format | Article |
| id | doaj.art-ec3de1bac41541e199f8d7936d1e2f62 |
| institution | Directory Open Access Journal |
| issn | 2571-8797 |
| language | English |
| last_indexed | 2024-03-09T17:10:49Z |
| publishDate | 2022-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Clean Technologies |
| spelling | doaj.art-ec3de1bac41541e199f8d7936d1e2f622023-11-24T14:04:49ZengMDPI AGClean Technologies2571-87972022-12-01441317132910.3390/cleantechnol4040081Temperature-Dependent Structure–Function Properties of Bacterial Xylose Isomerase Enzyme for Food Applications: An In Silico StudyMaurya Sharma0Naayaa Mehta1Renuka Suravajhala2Cynthia Meza3Shrabana Sarkar4Aparna Banerjee5Interfaculty Institute of Biochemistry (IFIB), Eberhard Karls University of Tübingen, 72074 Tübingen, GermanyBioclues, Hyderabad 500072, IndiaSchool of Biotechnology, Amrita Vishwa Vidyapeetam, Amritapuri, Kollam 690525, IndiaDoctorado en Biotecnología Traslacional (DBT), Facultad de Ciencias Agrarias y Forestales, Universidad Católica del Maule, Talca 3466706, ChileCentro de Investigación de Estudios Avanzados del Maule, Vicerrectoría de Investigación y Posgrado, Universidad Católica del Maule, Talca 3466706, ChileCentro de Investigación de Estudios Avanzados del Maule, Vicerrectoría de Investigación y Posgrado, Universidad Católica del Maule, Talca 3466706, ChileXylose Isomerase (XI) is an intramolecular oxidoreductase enzyme and catalyzes the reversible conversion of ketoses and aldoses in addition to the bioconversion of ethanol from xylose in the production of bioethanol from hemicellulose. It has a broad range of industrial applications in the food and pharmaceutical sectors, particularly in the production of the sweetener high fructose corn syrup (HFCS). It is one of the most widely used industrial enzymes after protease. Taking this into consideration, four bacterial XI sources were selected based on growth temperature, i.e., psychrophile, mesophile, thermophile, and hyperthermophile, for analyzing Xylose Isomerase’s structure-function characteristics. It was found that thermophilic XI was structurally less stable than mesophilic and hyperthermophilic XI, whereas structural plasticity ran opposite towards mesophiles. The interaction of xylose isomerase (XI) with two ligands, namely Amino-2-Hydroxymethyl-Propane-1,3-Diol and (4R)-2-Methylpentane-2,4- Diol, was also studied. Mesophilic XI demonstrated better binding affinity with structurally stabilizing amino acids (Ala, Asp, Gly, Leu, and Arg). In comparison, Thermophilic XI showed nearly similar binding affinity with both Amino-2-Hydroxymethyl-Propane-1,3-Diol and (4R)-2-Methylpentane-2,4-Diol. The results of this investigation suggest that thermophilic XI, followed by mesophilic XI, would be the most appropriate for establishing process stability and sustainability in the food industry.https://www.mdpi.com/2571-8797/4/4/81xylose isomerasetemperature dependencestructure–function analysesfood applications |
| spellingShingle | Maurya Sharma Naayaa Mehta Renuka Suravajhala Cynthia Meza Shrabana Sarkar Aparna Banerjee Temperature-Dependent Structure–Function Properties of Bacterial Xylose Isomerase Enzyme for Food Applications: An In Silico Study Clean Technologies xylose isomerase temperature dependence structure–function analyses food applications |
| title | Temperature-Dependent Structure–Function Properties of Bacterial Xylose Isomerase Enzyme for Food Applications: An In Silico Study |
| title_full | Temperature-Dependent Structure–Function Properties of Bacterial Xylose Isomerase Enzyme for Food Applications: An In Silico Study |
| title_fullStr | Temperature-Dependent Structure–Function Properties of Bacterial Xylose Isomerase Enzyme for Food Applications: An In Silico Study |
| title_full_unstemmed | Temperature-Dependent Structure–Function Properties of Bacterial Xylose Isomerase Enzyme for Food Applications: An In Silico Study |
| title_short | Temperature-Dependent Structure–Function Properties of Bacterial Xylose Isomerase Enzyme for Food Applications: An In Silico Study |
| title_sort | temperature dependent structure function properties of bacterial xylose isomerase enzyme for food applications an in silico study |
| topic | xylose isomerase temperature dependence structure–function analyses food applications |
| url | https://www.mdpi.com/2571-8797/4/4/81 |
| work_keys_str_mv | AT mauryasharma temperaturedependentstructurefunctionpropertiesofbacterialxyloseisomeraseenzymeforfoodapplicationsaninsilicostudy AT naayaamehta temperaturedependentstructurefunctionpropertiesofbacterialxyloseisomeraseenzymeforfoodapplicationsaninsilicostudy AT renukasuravajhala temperaturedependentstructurefunctionpropertiesofbacterialxyloseisomeraseenzymeforfoodapplicationsaninsilicostudy AT cynthiameza temperaturedependentstructurefunctionpropertiesofbacterialxyloseisomeraseenzymeforfoodapplicationsaninsilicostudy AT shrabanasarkar temperaturedependentstructurefunctionpropertiesofbacterialxyloseisomeraseenzymeforfoodapplicationsaninsilicostudy AT aparnabanerjee temperaturedependentstructurefunctionpropertiesofbacterialxyloseisomeraseenzymeforfoodapplicationsaninsilicostudy |