In silico and in vitro comparison of nicotinamide adenine dinucleotide phosphate dependent xylose reductase rossmaan fold in Debaryomycetaceae yeast family

Abstract

abstract Meyerozyma caribbica is prominently used for the production of xylitol from agro waste hydrolysate of the corncob. M. caribbica was isolated from fermented apple juice, the nicotinamide adenine dinucleotide phosphate (NADP) dependent xylose reductase (XR) enzyme act as a catalyst for the production of xylitol from xylose during xylose fermentation by M. caribbica. The enzyme XR was extracted, partially purified, sequenced and molecular weight was determined by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF). This study explores the in silico and in vitro comparative analysis of the cofactor NADP binding mechanism in rossmann fold of isolated M. caribbica and other xylose fermenting Debaryomycetaceae family yeast. The rossmaan fold analysis of M. caribbica and Debaryomycetaceae family of yeast revealed, xylose fermenting organisms such as Scheffersomyces stipitis, Debaryomyces hansenii, Debaryomyces nepalensis, Candida parapsilosis, Candida maltosa have divergence structure of rosmann fold. Whereas M. caribbica and Candida tenuis has unique structure of rossmann fold. Also, the identified rossmann fold of Debaryomycetaceae family yeast and isolated M. caribbica are conserved to interact with cofactor NADP by H2 bonding, which displays the proximity evolutionary relationship of the enzyme in Debaryomycetaceae family yeast. Annotation analysis showed the isolated M. caribbica has the ability of aldopentose fermentation for xylitol production.