Location: Renewable Product Technology ResearchTitle: Novel sources of ß-glucanase for the enzymatic degradation of schizophyllan Author
|Leathers, Timothy - Tim|
|Peterson, Stephen - Steve|
Submitted to: Enzyme and Microbial Technology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 12/4/2012
Publication Date: 12/10/2012
Publication URL: http://handle.nal.usda.gov/10113/62043
Citation: Sutivisedsak, N., Leathers, T.D., Bischoff, K.M., Nunnally, M.S., Peterson, S.W. 2013. Novel sources of ß-glucanase for the enzymatic degradation of schizophyllan. Enzyme and Microbial Technology. 52(3):203-210. Interpretive Summary: In this research we discovered novel sources of enzymes for the degradation of the biopolymer, schizophyllan. Although schizophyllan is commercially produced for pharmaceutical and cosmetics uses, surprisingly little information is available on the degradation of the polymer; enzymes that attack schizophyllan could be useful for controlled modifications of the polymer for novel applications. We isolated novel fungal strains and characterized their enzymes for the degradation of schizophyllan. This information will enable researchers to develop new uses for schizophyllan.
Technical Abstract: Schizophyllan is a homoglucan produced by the fungus Schizophyllum commune, with a ß-1,3-linked backbone and ß-1,6-linked side chains of single glucose units at every other residue. Schizophyllan is commercially produced for pharmaceutical and cosmetics uses. However, surprisingly little information is available on the biodegradation of schizophyllan. Enzymes that attack schizophyllan could be useful for controlled modifications of the polymer for novel applications. Enrichment cultures were used to isolate 20 novel fungal strains from soil samples, capable of growing on schizophyllan as a sole carbon source. Three additional strains were isolated as contaminants of stored schizophyllan solutions. Strains showing the highest levels of ß-glucanase activity were identified as Penicillium simplicissimum, P. crustosum, and Hypocrea nigricans. ß-glucanases also showed activity against the similar ß-glucans, laminarin and curdlan. By comparison, commercial ß-glucanase from Trichoderma longibrachiatum and laminarinase from Trichoderma sp. showed lower specific activities toward schizophyllan than most of the novel isolates. ß glucanases from P. simplicissimum and H. nigricans exhibited temperature optima of 60 ºC and 50 ºC against schizophyllan, respectively, with broad pH optima around pH 5.0. Partial purifications of ß-glucanase from P. simplicissimum and P. crustosum demonstrated the presence of multiple active endoglucanase species, including a 20-25 kDa enzyme from P. simplicissimum.