Production and partial characterization of extracellular peroxidase produced byStreptomyces sp. F6616 isolated in Turkey

Abstract

-Streptomyces sp. F6616 was found to produce higher levels of extracellular peroxidase activity (0.535 U/ mL) without any inducers than other actinobacteria which are previously reported. Maximum specific peroxidase activity (6.21 U/mg of protein) was obtained after 72 h of incubation at 30 °C in a minimal salt medium (pH 8.0) containing (in wt/v) 0.6% yeast extract and 0.8% ball-milled wheat straw corresponding to a C:N ratio of 4.6:1. Characterization of the peroxidase revealed that the optimal temperature for the enzyme activity, using the standard 2,4-dichlorophenol (2,4-DCP) assay was 50 °C, when the enzyme reaction was performed at pH 8.0. A study of the effect of temperature on the stability of peroxidase over time, showed that the enzyme was stable at 50 °C, with a half-life of 145 min, while at higher temperature the stability and activity was reduced such that at 60 °C the half-life of the enzyme was 30 min. The optimum pH for the activity of the enzyme occurred between pH 9.0 and 10.0. The apparent K m and V max values for the peroxidase preparations were determined to be 1.52 mmol/L and 1.84 U/mg protein, respectively using 2,4-DCP as a substrate. Characterization of the peroxidase activity revealed activity against 2,4-DCP, L-3,4-dihydroxyphenylalanine (L-DOPA), 2,4,5-trichlorophenol and other chlorophenols in the presence of hydrogen peroxide. However, inhibition of peroxidase activity with the addition of potassium cyanide and sodium azide, suggested the presence of heme component in the tertiary structure of the enzyme.

Controlling the simultaneous production of laccase and lignin peroxidase from Streptomyces cinnamomensis by medium formulation

“…F2621 and F6616 [16], Streptomyces viridosporus [25], Streptomyces albus [26], Botryosphaeria rhodina [27], Pleurotus ostreatus and Pleurotus sajorcaju [28], and Streptomyces lavendulae [5]. …”

Isolation and characterization of humic substances‐degrading bacteria from the subarctic Alaska grasslands

“…Several different soil bacteria have been isolated and characterized based on their capacity to metabolize HA, a principal component of HS, and lignin, a suitable surrogate of biopolymer HS in lab experiments. It was reported that biodegradation of HA and lignin by soil Streptomyces strains and a Novosphingobium sp., respectively, is associated with extracellular peroxidase [7,8] and/or laccase activity [9]. However, bacterial degradation of HS in cold environments remained unexplored and was the impetus for the present study.…”

Agrowastes utilization by Raoultella ornithinolytica for optimal extracellular peroxidase activity

“…Given the high‐utility potential of peroxidases, large‐scale production is of utmost importance to the bioeconomy, besides, an effective biocatalytic process requires enhanced enzyme activity and production systems. The production of extracellular peroxidases by some bacteria has been reported . However, most of these reports are on actinomycetes, predominantly Streptomyces species.…”