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One of the major constraints limiting the use of abundantly available lignocellulosic biomass as potential feedstock for alcohol industry is the lack of C 6 /C 5  co-sugar fermenting yeast. The present study explores a mutant yeast  Pichia kudriavzevii  BGY1-γm as a potential strain for bioconversion of glucose/xylose sugars of green biomass into ethanol under batch fermentation. The mutant strain having higher alcohol dehydrogenase activity (11.31%) showed significantly higher ethanol concentration during co-fermentation of glucose/xylose sugars (14.2%) as compared to the native strain. Based on 99% sequence similarity of ADH encoding gene from the mutant with the gene sequences from other yeast strains, the ADH enzyme was identified as ADH-1 type. The study reveals first three-dimensional model of ADH-1 utilizing glucose/xylose sugars from  P. kudriavzevii  BGY1-γm ( Pk ADH mutant). The refined and validated model of  Pk ADH mutant was used for molecular docking against the substrate (acetaldehyde) and product (ethanol). Molecular docking results showed that substrate and product exhibited a binding affinity of −4.55 and −4.5 kcal/mol with  Pk ADH mutant. Acetaldehyde and ethanol interacted at the active site of  Pk ADH mutant via hydrogen bonds (Ser42, His69 and Asp163) and hydrophobic interactions (Cys40, Ser42, His69, Cys95, Trp123 and Asp163) to form the stable protein–ligand complex. Molecular dynamics analysis revealed that  Pk ADH-mutant acetaldehyde and  Pk ADH-mutant ethanol complexes were more stable than  Pk ADH mutant. MMPBSA binding energy confirmed that binding of substrate and product results in the formation of a lower energy stable protein–ligand complex. Communicated by Ramaswamy H. Sarma

journal of biomolecular structure and dynamics

Molecular modeling and dynamics simulation of alcohol dehydrogenase enzyme from high efficacy cellulosic ethanol-producing yeast mutant strain  Pichia kudriavzevii  BGY1-γm