4.5 Article

Novel sources of β-glucanase for the enzymatic degradation of schizophyllan

Journal

ENZYME AND MICROBIAL TECHNOLOGY
Volume 52, Issue 3, Pages 203-210

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2012.12.002

Keywords

beta-glucanase; Hypocrea nigricans; Penicillium simplicissimum; Penicillium crustosum; Schizophyllum commune; Schizophyllan

Funding

  1. Agriculture and Food Research Initiative Competitive Grant from the USDA National Institute of Food and Agriculture [2010-65504-20377]
  2. NIFA [581328, 2010-65504-20377] Funding Source: Federal RePORTER

Ask authors/readers for more resources

Schizophyllan is a homoglucan produced by the fungus Schizophyllum commune, with a beta-1,3-linked backbone and beta-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 beta-glucanase activity were identified as Penicillium simplicissi mum, crustosum, and Hypocrea nig-ricans. beta-glucanases also showed activity against the similar beta-glucans, laminarin and curdlan. By comparison, commercial beta-glucanase from Trichoderma longibrachiatum and laminarinase from Trichoderma sp. showed lower specific activities toward schizophyllan than most of the novel isolates. beta-glucanases from P. simplicissimum and H. nigri cans exhibited temperature optima of 60 degrees C and 50 degrees C against schizophyllan, respectively, with broad pH optima around pH 5.0. Partial purifications of beta-glucanase from P. simplicissimum and P. crustosum demonstrated the presence of multiple active endoglucanase species, including a 20-25 kD enzyme from P. simplicissimum. Published by Elsevier Inc.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available