title: Thermotolerant hemicellulolytic and cellulolytic enzymes from Eupenicillium parvum 4-14 display high efficiency upon release of ferulic acid from wheat bran.
abstract: OBJECTIVE
  To characterize the hemicellulolytic and cellulolytic enzymes from novel fungi, and evaluate the potential of novel enzyme system in releasing ferulic acid (FA) from biomass resource.
  
  
  RESULTS
  A hemicellulolytic and cellulolytic enzyme-producing fungus 4-14 was isolated from soil by Congo red staining method, and identified as Eupenicillium parvum based on the morphologic and molecular phylogenetic analysis. The optimum temperature of fungal growth was 37°C. Hemicellulolytic and cellulolytic enzymes were produced by this fungus in solid-state fermentation (SSF), and their maximum activities were 554, 385, 218, 2·62 and 5·25 U g(-1) for CMCase, xylanase, β-glucosidase, FPase and FAE respectively. These enzymes displayed the best catalytic ability at low pH values (pH 4·5-5·0). The optimum temperatures were 70°C, 70°C, 75°C and 55°C for CMCase, β-glucosidase, xylanase and FAE respectively. CMCase, xylanase and FAE were stable at different pHs or high temperature (60°C). Enzymatic hydrolysis experiment indicated that the maximum (76·8 ± 4)% of total alkali-extractable FA was released from de-starched wheat bran by the fungal enzyme system.
  
  
  CONCLUSIONS
  High activities of thermotolerant CMCase, β-glucosidase, xylanase and FAE were produced by the newly isolated fungus E. parvum 4-14 in SSF. The fungal enzyme system displayed high efficiency at releasing FA from wheat bran.
  
  
  CONCLUSIONS
  This study provides a new fungal strain for researches of novel hemicellulolytic and cellulolytic enzymes and will improve the bioconversion and utilization of agricultural by-products.
authors.affiliation: College of Chemical Engineering, Nanjing Forestry University, Nanjing, China.
authors.forename: L
authors.initials: L
authors.lastname: Long
authors.affiliation: College of Chemical Engineering, Nanjing Forestry University, Nanjing, China.
authors.forename: D
authors.initials: D
authors.lastname: Ding
authors.affiliation: College of Chemical Engineering, Nanjing Forestry University, Nanjing, China.
authors.forename: Z
authors.initials: Z
authors.lastname: Han
authors.affiliation: College of Chemical Engineering, Nanjing Forestry University, Nanjing, China.
authors.forename: H
authors.initials: H
authors.lastname: Zhao
authors.affiliation: Nanjing Institute for the Comprehensive Utilization of Wild Plants, Nanjing, China.
authors.forename: Q
authors.initials: Q
authors.lastname: Lin
authors.affiliation: College of Chemical Engineering, Nanjing Forestry University, Nanjing, China.
authors.forename: S
authors.initials: S
authors.lastname: Ding
mesh_terms: D002480:Cellulase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003373:Coumaric Acids / Q000032:analysis* / Q000378:metabolism; D004043:Dietary Fiber / Q000032:analysis / Q000378:metabolism*; D055324:Eupenicillium / Q000737:chemistry / Q000145:classification / Q000201:enzymology* / Q000235:genetics; D005285:Fermentation; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D010802:Phylogeny; D013696:Temperature; D001617:beta-Glucosidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D003373:Coumaric Acids; D004043:Dietary Fiber; D005656:Fungal Proteins; C004999:ferulic acid; D001617:beta-Glucosidase; D002480:Cellulase; C019826:carboxymethylcellulase
keywords: Eupenicillium parvum; cellulase; feruloyl esterases; thermophilic enzyme; xylanase