Abstract
The highest production of α-L-arabinofuranosidase by Penicillium janczewskii in medium with brewer’s spent grain and orange waste was observed when cultivation was carried out in pH 5.0 at 25°C, for 8.5 days under shaking. The α-L-arabinofuranosidase present in the crude filtrate was optimally active at 60°C and pH 4.0; it was stable in a wide range of pH, maintaining 90% of the activity from 2.0 to 8.0. The enzyme was very stable at 40°C, maintaining 90% of the activity within 1 h. The estimated half-life at 50°C was 10 min, and at 60 and 70°C, it was 5 min. This enzyme was activated in the presence of Ba2+, Ca2+, Mn2+ and NH4+ while the ions Pb2+, Mg2+, Hg2+, Co2+ and Cu2+, as well as PMSF, DTT, β-mercaptoethanol, EDTA and SDS inhibited it. Key words: α-L-Arabinofuranosidase, Penicillium janczewskii, enzyme production, enzyme properties, industrial wastes.
Highlights
Arabinosyl residues are largely distributed in the side chains of some hemicelluloses, especially arabinoxylans.Usually, the presence of side chains can restrict the full enzymatic hydrolysis of hemicelluloses, preventing the complete degradation of these polymers (Numan and Bhosle, 2006; Peng et al, 2012).Due to xylans heterogeneity and complexity, an enzymatic complex is required for their complete hydrolysis
When P. janczewskii was cultivated in different temperatures (Figure 1), the highest ABF production was verified at 25°C (0.10 U/mL), intermediate values were observed at 20 and 30°C (0.04 and 0.09 U/mL, respectively), and no activity was verified at 35°C
Brasilianum and P. purpurogenum was observed in intermediate temperatures (27-28°C)
Summary
Arabinosyl residues are largely distributed in the side chains of some hemicelluloses, especially arabinoxylans.Usually, the presence of side chains can restrict the full enzymatic hydrolysis of hemicelluloses, preventing the complete degradation of these polymers (Numan and Bhosle, 2006; Peng et al, 2012).Due to xylans heterogeneity and complexity, an enzymatic complex is required for their complete hydrolysis. Arabinosyl residues are largely distributed in the side chains of some hemicelluloses, especially arabinoxylans. The presence of side chains can restrict the full enzymatic hydrolysis of hemicelluloses, preventing the complete degradation of these polymers (Numan and Bhosle, 2006; Peng et al, 2012). Α-L-arabinofuranosidases (EC 3.2.1.55) are responsible to hydrolyze non-reducing ends of α-L-1,2-, α-L-1,3- and α-L-1,5-arabinofuranosyl residues of many branched oligo- and polysaccharides, especially those containing large amounts of arabinose, as arabinoxylans (found in cereal grain and softwood), arabinan and other polysaccharides containing L-arabinose (Saha, 2000; Numan and Bhosle, 2006; Seiboth and Metz, 2011). The production of α-L-Arabinofuranosidases (ABF) can be observed in several microorganisms, as bacteria and fungi, and in some plants (Lagaert et al, 2014). The production of theses enzymes by microorganisms is strongly influenced by the composition of the culture medium, mainly in relation to the carbon source
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