Additional file 1: Table S1. of Biochemical characterization and synergism of cellulolytic enzyme system from Chaetomium globosum on rice straw saccharification

Comparison of cellulose production by C. globosum BCC5776 and other fungi in recent selected publications. (DOCX 16 kb

Additional file 2: Table S2. of Biochemical characterization and synergism of cellulolytic enzyme system from Chaetomium globosum on rice straw saccharification

Sugar yields from hydrolysis of pretreated rice straw using various enzyme combinations and dosages. (DOCX 15 kb

Production of high activity <i>Aspergillus niger</i> BCC4525 β-mannanase in <i>Pichia pastoris</i> and its application for mannooligosaccharides production from biomass hydrolysis

<p>A cDNA encoding β-mannanase was cloned from <i>Aspergillus niger</i> BCC4525 and expressed in <i>Pichia pastoris</i> KM71. The secreted enzyme hydrolyzed locust bean gum substrate with very high activity (1625 U/mL) and a relatively high <i>k</i>_cat/<i>K</i>_<i>m</i> (461 mg⁻¹ s⁻¹ mL). The enzyme is thermophilic and thermostable with an optimal temperature of 70 °C and 40% retention of endo-β-1,4-mannanase activity after preincubation at 70 °C. In addition, the enzyme exhibited broad pH stability with an optimal pH of 5.5. The recombinant enzyme hydrolyzes low-cost biomass, including palm kernel meal (PKM) and copra meal, to produce mannooligosaccharides, which is used as prebiotics to promote the growth of beneficial microflora in animals. An <i>in vitro</i> digestibility test simulating the gastrointestinal tract system of broilers suggested that the recombinant β-mannanase could effectively liberate reducing sugars from PKM-containing diet. These characteristics render this enzyme suitable for utilization as a feed additive to improve animal performance.</p> <p>A recombinant β-mannanase from <i>A. niger</i> BCC4525 exhibits high activity. It produces MOS from low-cost biomass and enhance the release of reducing sugars from diet.</p

Characterization of cellulolytic enzyme system of <i>Schizophyllum commune</i> mutant and evaluation of its efficiency on biomass hydrolysis

<p><i>Schizophyllum commune</i> is a basidiomycete equipped with an efficient cellulolytic enzyme system capable of growth on decaying woods. In this study, production of lignocellulose-degrading enzymes from <i>S. commune</i> mutant G-135 (SC-Cel) on various cellulosic substrates was examined. The highest cellulase activities including CMCase, FPase, and β-glucosidase were obtained on Avicel-PH101 while a wider range of enzymes attacking non-cellulosic polysaccharides and lignin were found when grown on alkaline-pretreated biomass. Proteomic analysis of SC-Cel also revealed a complex enzyme system comprising seven glycosyl hydrolase families with an accessory carbohydrate esterase, polysaccharide lyase, and auxiliary redox enzymes. SC-Cel obtained on Avicel-PH101 effectively hydrolyzed all agricultural residues with the maximum glucan conversion of 98.0% using corn cobs with an enzyme dosage of 5 FPU/g-biomass. The work showed potential of SC-Cel on hydrolysis of various herbaceous biomass with enhanced efficiency by addition external β-xylosidase.</p> <p>Enzymatic hydrolysis of alkaline-pretreated biomass by Sc-Cel and yield enhancement by external β-xylosidase (BX).</p