Abo Bibliothek: Guest
Digitales Portal Digitale Bibliothek eBooks Zeitschriften Referenzen und Berichte Forschungssammlungen
International Journal of Medicinal Mushrooms
Impact-faktor: 1.423 5-jähriger Impact-Faktor: 1.525 SJR: 0.431 SNIP: 0.661 CiteScore™: 1.38

ISSN Druckformat: 1521-9437
ISSN Online: 1940-4344

Volumes:
Volumen 22, 2020 Volumen 21, 2019 Volumen 20, 2018 Volumen 19, 2017 Volumen 18, 2016 Volumen 17, 2015 Volumen 16, 2014 Volumen 15, 2013 Volumen 14, 2012 Volumen 13, 2011 Volumen 12, 2010 Volumen 11, 2009 Volumen 10, 2008 Volumen 9, 2007 Volumen 8, 2006 Volumen 7, 2005 Volumen 6, 2004 Volumen 5, 2003 Volumen 4, 2002 Volumen 3, 2001 Volumen 2, 2000 Volumen 1, 1999

International Journal of Medicinal Mushrooms

DOI: 10.1615/IntJMedMushr.v15.i5.80
pages 505-515

Mycelial Biomass and Biochemical Properties of Proteases Produced by Lentinus citrinus DPUA 1535 (Higher Basidiomycetes) in Submerged Cultivation

Larissa de Souza Kirsch
Culture Collection DPUA/UFAM, Federal University of Amazon, Manaus, AM, Brazil
Valeria de Carvalho Santos Ebinuma
Department of Bioprocess and Biotechnology, School of Pharmaceutical Sciences, UNESP-Univ. Estadual Paulista, Araraquara, Brazil
Maria Francisca Simas Teixeira
Culture Collection DPUA/UFAM, Federal University of Amazon, Manaus, AM, Brazil

ABSTRAKT

The cultivation of Lentinus citrinus for mycelial biomass and protease production under different carbon and nitrogen sources was studied in submerged cultivation. The nutritional source concentration for protease production was evaluated using a full factorial design. For mycelial biomass maltose (4.94 mg/mL) and beef extract (5.45 mg/mL), carbon and nitrogen sources presented the best results, respectively. The maximum protease activity was 73.33 U/mL with fructose (30.0 g/L) and beef extract (10.0 g/L). Proteases showed maximum activity at 40°C and pH 7.0, which exhibited high stability at experimental conditions. The final part of this work was devoted to estimating the main thermodynamic parameters of the irreversible enzyme inactivation (ΔH* = 17.86 kJ/mol, ΔG* =102.09 kJ/mol, ΔS* = −260.76 J/mol×K) through residual activity tests carried out at 25−70°C, by making use of Arrhenius and Eyring plots.