Middle-redox potential laccase from Ganoderma sp.: its application in improvement of feed for monogastric animals

Abstract

The variables influencing laccase production by white-rot fungus Ganoderma sp. rckk-02 were optimized employing response surface methodology. Malt extract (6.0% w/v), lignin (0.5% w/v) and pH (5.5) were found to be the most significant factors for enhanced laccase production by 7 fold (226.0 U/ml) as compared to unoptimized growth conditions (32.0 U/ml). The N-terminal sequence of laccase revealed its distinct amino acid profile (S- I- R- N- S- G), which suggested it as a novel enzyme. The Far-UV CD spectrum of the laccase showed single broad negative trough at around 213 nm, a typical signature of all β proteins. The laccase was found to fall in the range of middle redox potential laccases. Purified laccase at dosage of 2.5 Ug−1 body weight when supplemented with pelleted diet of rats, a significant improvement (p < 0.05) in nutrients digestibility without causing any elevation of blood stress enzymes was observed.

Assessing the tolerance of immobilized laccase from a salt-tolerant strain of Trichoderma viride Pers NFCCI-2745 to heavy metal ions, detergents and copper chelating agents

“…The effect of detergents on immobilized laccase was not reported earlier. In contrast to earlier studies reported on free enzymes (Laufer et al 2006;Sharma et al 2013), SDS decreased the enzymatic activity of immobilized laccase at concentrations higher than 2 mM. This study for the first time demonstrates the effect of detergents on immobilized laccase.…”

“…Recent study on purified laccase from Ganoderma sp. has shown maximum inhibition of laccase with CoCl 2 and HgCl 2 and stability in presence of CaCl 2 , MnSO 4 , FeCl 3 , ZnSO 4 and BaCl 2 (0.5-3 mM) with a significant inhibition only at 10 mM of the metal ions (Sharma et al 2013). However, the effect of metal ions on immobilized laccase was not reported earlier.…”

“…CTAB (t = 7.327 df = 10, P value = 0.0001) and Tween 20 (t = 8.201 df = 10, P value = 0.0001) significantly increased the activity of Ba-Cu alginate beads compared to other detergents tested. A very recent study by Sharma et al (2013) has shown moderate stability of purified laccase to surfactant, Triton X-100 and all tweens (except Tween 20), SDS and CTAB at 5 and 10 mM concentration. Immobilized beads showed tolerance to all detergents analyzed except SDS even at a high concentration of 10 mM.…”

Laccase isozymes from Ganoderma lucidum MDU-7: Isolation, characterization, catalytic properties and differential role during oxidative stress

“…Recent, whole genome sequence of G. lucidum has revealed complete set of ligninolytic peroxidases, laccases and cellobiose dehydrogenases, which makes it excellent model for ligninolytic enzymatic studies [2]. Earlier, Ganoderma has been reported with different lignin modifying enzymes, such as, manganese-dependent peroxidase (MnP) and laccase [3,4]. Laccases (p-diphenol: dioxygen oxidoreductase; EC 1.10.3.2) are polyphenol oxidases that catalyze the oxidation of phenolic compounds with a concomitant reduction of oxygen to water [5].…”

The effects of hydrolysed sorghum on growth performance and meat quality of rabbits

“…However, the use of these lignocellulose-rich substrates, which can be made available by WRF metabolism, is limited in ruminant nutrition (Sarnklong et al, 2010;Millati et al, 2011). As a result, limited research has been conducted concerning the use of lignocellulose-rich substrates in monogastric animal diets (Shrivastava et al, 2011;Sharma et al, 2013;Shrivastava et al, 2014). Although some studies have evaluated lignocellulose-rich substrate use in order to increase the nutritional value of different agroindustrial wastes, few have examined the effects of WRF-hydrolysed ingredients on production traits and rabbit meat quality (Brozzoli et al, 2010;Shrivastava et al, 2011;Isikhuemhen et al, 2012;Tanemura et al, 2016).…”