Hydrolytic properties of crude alpha-L-rhamnosidases produced by several wild strains of mesophilic fungi

Abstract

Aims: Observation of the dependence of a-L-rhamnosidase activity on pH and temperature and the capability to hydrolyse concentrated naringin solutions and hesperidin suspensions of enzyme complexes produced by several fungi. Methods and Results: The enzymes were produced by several wild strains of mesophilic fungi grown in liquid media containing rhamnose as sole carbon source. The properties and their ranges of values measured were as follows: (i) optimum pH, 3AE5-6AE5; (ii) optimum temperature, 50-65°C; (iii) hydrolysis of supersaturated 100 g l )1 naringin solutions, 45-100% and (iv) hydrolysis of hesperidin suspensions, 6-35%. Conclusions: Some a-L-rhamnosidase enzymes hydrolysed supersaturated naringin solutions with a high yield. The enzyme produced by Fusarium sambucinum 310 showed good activity even at pH 10. Significance and Impact of the Study: Crude enzymes with possible utilization as catalysts for the manufacture of hydrolysis products of the flavonoid glycosides were found.

Production, partial purification and characterization of α-l-rhamnosidase from Penicillium ulaiense

“…3. The optimum pH (5.0) of P. ulaiense a-rhamnosidase was in the range reported for this enzyme produced by other fungi, between 3.4 and 6.5 (Romero et al 1985;Puri et al 1996;Soria et al 1999;Spagna et al 2000;Scaroni et al 2002). In that range of pH the activity was more than 60% of its maximum value (Fig.…”

“…3b); above that range the activity was highly sensitive to very small increases in temperature, and 90% of the activity at 65°C was lost at 75°C. The maximum activity for the P. ulaiense enzyme was observed between the higher values found for other fungal a-rhamnosidases (Gallego Custodio et al 1996;Manzanares et al 1997;Soria et al 1999;Scaroni et al 2002). An optimum temperature of 70°C was reported for this enzyme by Spagna et al (2000).…”

Production of Hesperetin Using a Covalently Multipoint Immobilized Diglycosidase from <b><i>Acremonium</i></b> sp. DSM24697

“…The hesperetin concentration yielded by the Ag-G αRβGl system was around 3.5 times higher than the system catalyzed by pectinase 62L (a bulk enzyme preparation), and 16-fold lower than a heterogeneous system that used supersaturated suspensions of hesperidin (16 m M ) as the substrate. However, the specific productivities were ∼ 25-and 37-fold lower, respectively, than the specific productivity found for the system herein presented ( table 3 ) [Mandalari et al, 2006;Scaroni et al, 2002]. Moreover, an additional advantage of the reaction catalyzed by Ag-G αRβGl, besides the possibility of recycling it, is that it also coproduced another highly valuable product, the disaccharide rutinose.…”

“…Moreover, an additional advantage of the reaction catalyzed by Ag-G αRβGl, besides the possibility of recycling it, is that it also coproduced another highly valuable product, the disaccharide rutinose. This is in contrast to the sequential enzymatic mechanisms of deglycosylation involving two monoglycosidases, where the aglycone productivity becomes a more complex biotransformation composed of five chemical species (the substrate, rhamnose, glucose, the glucosylated aglycone and the aglycone) [Orrillo et al, 2007;Scaroni et al, 2002;Spagna et al, 2002]. Recently, a one-step process for rutin deglycosylation using a thermophile promiscuous β-glucosidase and releasing quercetin and rutinose was also reported.…”

Evaluation and characterization of new α-L-rhamnosidase-producing yeast strains

“…GL1 (Hashimoto et al, 1999), Lactobacillus plantarum NCC 245 (Avila et al, 2009), Aspergillus flavus (Scaroni et al, 2002), Curvularia lunata (Feng et al, 2007), Aspergillus niger (Puri and Kalra, 2005) and Aspergillus kawachii (Koseki et al, 2008). Enzymes from Pichia angusta (Yanai and Sato, 2000), Aspergillus kawachii, Penicillium aureatiogriseum and Trichoderma longibrachiatu (Scaroni et al, 2002) were optimally active at 40°C and 60°C. This phenomenon suggested that the temperature for the enzymatic hydrolysis of naringin and conversion of other flavonoids should be controlled under 50°C.…”