Enhanced production of industrial enzymes in Mucoromycotina fungi during solid-state fermentation of agricultural wastes/by-products

Acta Biol Hung. 2015 Sep;66(3):348-60. doi: 10.1556/018.66.2015.3.10.

Abstract

Cellulolytic, lipolytic and proteolytic enzyme production of zygomycetes Mucor corticolus, Rhizomucor miehei, Gilbertella persicaria and Rhizopus niveus were investigated using agro-industrial wastes as substrates. Solid-state cultures were carried out on untreated corn residues (stalk and leaf) as single substrate (SSF1) or corn residues and wheat bran in mixed fermentation (SSF2). Rapid production of endoglucanase (CMCase) was observed with maximal activity reaching after about 48-h fermentation, while cellobiohydrolase (CBH) and β-glucosidase enzymes generally had their peak after 72-h incubation. Highest filter paper degrading (FPase), CMCase, CBH and β-glucosidase activities obtained were (U g⁻¹ dss) 17.3, 74.1, 12.2 and 158.3, for R. miehei, G. persicaria, M. corticolus and Rh. niveus, respectively. M. corticolus proved to be the best lipolytic enzyme producer in SSF1 presenting 447.6 U g⁻¹ dss yield, while R. miehei showed 517.7 U g⁻¹ dss activity in SSF2. Rh. niveus exhibited significantly greater protease production than the other strains. Suc-AAPF-pNA hydrolyzing activities of this strain were 1.1 and 1.96 U g⁻¹ dss in SSF1 and SSF2, respectively. We conclude that the used corn stalk and leaf residues could potentially be applicable as strong inducers for cellulase and lipase production by Mucoromycotina fungi.

Keywords: Zygomycetes; corn stalk and leaf; hydrolytic enzymes; mixed fermentation; wheat bran.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cellulases / biosynthesis*
  • Dietary Fiber
  • Fungal Proteins / biosynthesis*
  • Mucorales* / enzymology
  • Mucorales* / growth & development
  • Peptide Hydrolases / biosynthesis*
  • Plant Leaves / chemistry
  • Zea mays / chemistry

Substances

  • Dietary Fiber
  • Fungal Proteins
  • Cellulases
  • Peptide Hydrolases