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Ćilerdžić, J., Stajić, M., Vukojević, J., and Lončar, N. (2014). "Intraspecific diversity in the production and characterization of laccase within Ganoderma lucidum," BioRes. 9(3), 5577-5587.

Abstract

Ganoderma lucidum has a well-developed ligninolytic enzyme system, where laccase is the dominant and sometimes only synthesizing enzyme, and therefore could find an application in the delignification of abundant plant raw materials and in food, feed, paper, and biofuel production. The questions that provided the goals for the present study were whether the profile of G. lucidum laccase depends on cultivation type and carbon source, as well as whether intraspecific diversity exists. Conditions of submerged cultivation proved more preferable for laccase activity compared with solid-state cultivations in all studied strains, while oak sawdust provided a better carbon source than wheat straw. Maximum laccase activity (7241.0 U/L) was measured on day 14 of oak sawdust submerged fermentation by strain BEOFB 431. Intraspecific diversity in synthesized proteins was more significant in wheat straw than in oak sawdust submerged fermentation. The profile of laccase isoforms was dependent on strain, plant residue, type, and period of cultivation. Four acidic laccase isoforms (pI 3.6) were detected in G. lucidum BEOFB 431 at the same cultivation point where maximal enzyme activity was measured.
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