Temperature-Dependent Structure–Function Properties of Bacterial Xylose Isomerase Enzyme for Food Applications: An In Silico Study

Maurya Sharma, Naayaa Mehta, Renuka Suravajhala, Cynthia Meza, Shrabana Sarkar and Aparna Banerjee ()
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Maurya Sharma: Interfaculty Institute of Biochemistry (IFIB), Eberhard Karls University of Tübingen, 72074 Tübingen, Germany
Naayaa Mehta: Bioclues, Hyderabad 500072, India
Renuka Suravajhala: School of Biotechnology, Amrita Vishwa Vidyapeetam, Amritapuri, Kollam 690525, India
Cynthia Meza: Doctorado en Biotecnología Traslacional (DBT), Facultad de Ciencias Agrarias y Forestales, Universidad Católica del Maule, Talca 3466706, Chile
Shrabana Sarkar: Centro de Investigación de Estudios Avanzados del Maule, Vicerrectoría de Investigación y Posgrado, Universidad Católica del Maule, Talca 3466706, Chile
Aparna Banerjee: Centro de Investigación de Estudios Avanzados del Maule, Vicerrectoría de Investigación y Posgrado, Universidad Católica del Maule, Talca 3466706, Chile

Clean Technol., 2022, vol. 4, issue 4, 1-13

Abstract: 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.

Keywords: xylose isomerase; temperature dependence; structure–function analyses; food applications (search for similar items in EconPapers)
JEL-codes: Q2 Q3 Q4 Q5 (search for similar items in EconPapers)
Date: 2022
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