Trends in the development and current perspective of thermostable bacterial hemicellulases with their industrial endeavors: A review

Hemicellulases are enzymes that hydrolyze hemicelluloses, common polysaccharides in nature. Thermophilic hemicellulases, derived from microbial strains, are extensively studied as natural biofuel sources due to the complex structure of hemicelluloses. Recent research aims to elucidate the catalytic principles, mechanisms and specificity of hemicellulases through investigations into their high-temperature stability and structural features, which have applications in biotechnology and industry. This review article targets to serve as a comprehensive resource, highlighting the significant progress in the field and emphasizing the vital role of thermophilic hemicellulases in eco-friendly catalysis. The primary goal is to improve the reliability of hemicellulase enzymes obtained from thermophilic bacterial strains. Additionally, with their ability to break down lignocellulosic materials, hemicellulases hold immense potential for biofuel production. Despite their potential, the commercial viability is hindered by their high enzyme costs, necessitating the development of efficient bioprocesses involving waste pretreatment with microbial consortia to overcome this challenge. [Display omitted] •Thermophilic hemicellulases have superior efficiency in hydrolyzing hemicelluloses.•They have catalytic and non-catalytic domains for efficient hydrolysis.•These biocatalysts exhibit versatility in substrate specificity.•Hemicellulases play a key role in industrial processes and biofuel production.•They have been recognized as green catalysts for sustainable industries.