Application of Xylanase from <I>Thermomyces lanuginosus </I>IOC-4145 for Enzymatic Hydrolysis of Corncob and Sugarcane Bagasse

Abstract

Xylanases have significant current and potential uses for several industries including paper and pulp, food, and biofuel. For the biofuel industry, xylanases can be used to aid in the conversion of lignocellulose to fermentable sugars (e.g., xylose). We investigated the thermophilic fungus Thermomyces lanuginosus was yielded for xylanase production and found that the highest activity (850 U/mL) was yielded after 96 h of semisolid fermentation. The enzyme was used for hydrolyzing agricultural residues with and without pretreatment. Such residues were characterized in relation to the maximum xylose content by total acid hydrolysis. The highest xylose yields realized by enzymatic hydrolysis were 24 and 52%, achieved by using 3000 U/g (dried material) of sugarcane bagasse and corncob, respectively, which received both alkali and thermal pretreatment.

A novel thermostable xylanase GH10 from Malbranchea pulchella expressed in Aspergillus nidulans with potential applications in biotechnology

“…Consequently, the percentage of sugar release was very close to that observed using BIN (3.7% with BAS compared to 3.8% with BIN). It is noteworthy that previous reports using the xylanase from Thermomyces lanuginosus [ 21 ] reported a maximum of 2.6% hydrolysis using sugarcane bagasse submitted to thermal (steam explosion) pretreatment, a value much lower than the 41.5% observed in the current study.…”

“…MpXyn10A also has a cellulose-binding domain, and for this the cellulose-binding module (CBM1) of the endoglucanase I from Trichoderma reesei (PDB code 4BMF [ 20 ]) was used as a template. The templates thus identified, GH10 XYLANASE from Fusarium oxysporum (PDB code 3U7B [ 5 ]) and a cellulose-binding domain (CBD) of endoglucanase I from Trichoderma reesei (PDB code 4BMF [ 11 ]) were used for building a structural model of the XYN10A by comparative modeling techniques with the program MODELLER9v12 [ 21 ].…”

A Highly Thermostable Alkaline Cellulase-Free Xylanase from Thermoalkalophilic Bacillus sp. JB 99 Suitable for Paper and Pulp Industry: Purification and Characterization

“…The potential use of these xylanase is its selective removal of only hemicellulose component with minimal damage to cellulose pulp, which is of tremendous importance in pulp bleaching to avoid drop in quality of paper pulp. The industry highly demands for high alkaline (pH 8.0-10.0) and thermostable xylanase (70-80°C), which are employed in bleaching of paper pulp and conversion of agricultural residues into valuable by-products for bioethanol production [1,8,9,15]. However, completed nucleotide sequence of xylanase encoding gene from Bacillus sp.…”

Entrapment of Xylanase within a Polyethylene Glycol Net-Cloth Grafted on Polypropylene Nonwoven Fabrics with Exceptional Operational Stability and Its Application for Hydrolysis of Corncob Hemicelluloses

“…The complete enzymatic hydrolysis of hemicelluloses requires the synergistic actions of endo-β-1,4-xylanase (xylanase, EC 3.2.1.8), β-xylosidase (EC 3.2.1.37), and a series of enzymes that degrade side-chain groups. , Among these, endo-β-1,4-xylanase acts as the key role that cleaves internal β-1,4-xylan links to short-chain xylooligosaccharides of various lengths. β-Xylosidase catalyzes the hydrolysis of xylooligosaccharides to liberate xylose, and other accessory enzymes, such as acetyl xylan esterase (EC 3.1.1.73), α-glucuronidase (EC 3.2.1.139), and α-L-arabinofuranosidase (EC 3.2.1.55), act to accomplish complete hydrolysis. , …”