Abstract
UV-49, the mutant ofPenicillium funiculosum, showed higher production of cellulase although the specific activity with regards to filter paper activity was unaltered (0.7 U/mg). Fractionation of culture filtrates by isoelectric focusing indicated the presence of three endoglucanases and two β-glucosidases in the parent strain, whereas one endoglucanase and one β-glucosidase for UV-49. The thermostability of activity towards filter paper, CM-cellulose and ρ-nitrophenyl-β-D-glucoside of the parent strain was about 30–50% more than the corresponding activities of the mutant. The saccharification of bagasse with the enzymes from parent (66%) and mutant (62%) was comparable. However, the recovery of enzyme from residual cellulose was 10–20% less in case of the mutant. The formation of higher oligosaccharides in the hydrolysates of UV-49 on prolonged incubation indicated the presence of transglycosylation activity in the enzyme complex. In contrast the parent strain produces glucose; the desired end product of the practical saccharification.
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Rao, M., Lachke, A., Seeta, R. et al. Evaluation of cellulase complex ofPenicillium funiculosum and its mutant UV-49 in relation to practical saccharification. Appl Biochem Biotechnol 16, 25–34 (1987). https://doi.org/10.1007/BF02798353
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DOI: https://doi.org/10.1007/BF02798353