Functional expression and characterization of a glucuronoyl esterase from the fungus Neurospora crassa: identification of novel consensus sequences containing the catalytic triad

• Published in: Journal of general and applied microbiology Vol. 62; no. 5; pp. 217 - 224
• Main Authors: Huynh, Hung Hiep, Arioka, Manabu
• Format: Journal Article
• Language: English
• Published: Japan Applied Microbiology, Molecular and Cellular Biosciences Research Foundation 01.01.2016
• Subjects: Amino Acid Sequence; carbohydrate esterase family 15; Catalysis; Catalytic Domain; Consensus Sequence; Esterases - chemistry; Esterases - genetics; Esterases - isolation & purification; Esterases - metabolism; Fungal Proteins - chemistry; Fungal Proteins - metabolism; Glucuronic Acid - metabolism; glucuronoyl esterase; hemicellulose; Hydrolysis; Lignin - metabolism; lignin-carbohydrate complex; Neurospora crassa; Neurospora crassa - enzymology; Neurospora crassa - genetics; Neurospora crassa - metabolism; Oligopeptides - chemistry; Oligopeptides - metabolism; Pichia - genetics; Polysaccharides - metabolism; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; Substrate Specificity

The complete hydrolysis of lignocellulose requires the actions of a variety of enzymes, including those that cleave the linkage between lignin and hemicellulose. The enzyme glucuronoyl esterase (GE) that constitutes a novel family of carbohydrate esterases, CE15, has been shown to display a unique a...