دورية أكاديمية

Evaluation of hollocelulase production by Lentinula edodes (Berk.) Pegler during the submerged fermentation growth using RSM

التفاصيل البيبلوغرافية
العنوان: Evaluation of hollocelulase production by Lentinula edodes (Berk.) Pegler during the submerged fermentation growth using RSM
المؤلفون: Chicatto, JA, Costa, A, Nunes, H, Helm, CV, Tavares, LBB
المصدر: Brazilian Journal of Biology. February 2014 74(1)
بيانات النشر: Instituto Internacional de Ecologia, 2014.
سنة النشر: 2014
مصطلحات موضوعية: basidiomycetes, sugar cane bagasse, ammonium sulfate, hydrolytic enzymes, proteins
الوصف: The cellulase proteins have a great importance in the enzymatic hydrolysis of woody biomass. Despite of costs being a major concern, it has been a stimulus to study basidiomycetes biochemical properties which degrade lignocellulosic material and have prompted the processes' study for obtaining cellulolytic enzymes in fungi. The objective of this research was to evaluate the effects of the initial nitrogen content on (ammonium sulfate) and on sugar cane bagasse, which hereby, acts as an inducer of hydrolytic enzymes to produce cellulases and xylanases, using three Lentinula edodes (Berk.) Pegler strains as a transformation agent. A factorial design with 22 replications in the central point was conducted, varying concentrations of ammonium sulfate and sugar cane bagasse. The submerged cultures carried out in synthetic culture medium and incubated at 25°C for 7 days on an orbital shaker at 150 rpm. The total protein and cellulase activity as endoglucanase, exoglucanase and β-glucosidase and the xylanase was also determined. The results showed that the production of hydrolytic enzymes was stimulated by the presence of high concentrations of sugar cane bagasse (30g/L), characterizing it as an inducer due to the demonstrated proportional relationship. Thus, ammonium sulfate acted as a reducing agent in the synthesis of enzymes, being the low concentrations (0.1g/L) indicated for the enzyme production system under study. Among the studied strains, the EF52 showed higher activity for xylanase, endoglucanases, β-glucosidase and also protein.
نوع الوثيقة: article
وصف الملف: text/html
اللغة: English
تدمد: 1519-6984
DOI: 10.1590/1519-6984.21712
URL الوصول: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842014000100032
حقوق: info:eu-repo/semantics/openAccess
رقم الأكسشن: edssci.S1519.69842014000100032
قاعدة البيانات: SciELO
الوصف
تدمد:15196984
DOI:10.1590/1519-6984.21712