TY - JOUR
T1 - Bioprospecting of novel peroxidase from Streptomyces coelicolor strain SPR7 for carcinogenic azo dyes decolorization
AU - Preethi, P. Sai
AU - Vickram, Sundaram
AU - Das, Raja
AU - Hariharan, N. M.
AU - Rameshpathy, M.
AU - Subbaiya, R.
AU - Karmegam, N.
AU - Kim, Woong
AU - Govarthanan, M.
N1 - Publisher Copyright:
© 2022 Elsevier Ltd
PY - 2023/1
Y1 - 2023/1
N2 - Peroxidase (POX) is a heme-containing oxidoreductase, its voluminous immuno-diagnostic and bioremediatory intuitions have incited optimization and large scale-generation from novel microbial repertoires. Azo dyes are the most detrimental classes of synthetic dyes and they are the common ecotoxic industrial pollutants in wastewater. In addition, azo dyes are refractory to degradation owing to their chemical nature, comprising of azoic linkages, amino moieties with recalcitrant traits. Moreover, they are major carcinogenic and mutagenic on humans and animals, whereby emphasizing the need for decolorization. In the present study, a novel POX from Streptomyces coelicolor strain SPR7 was investigated for the deterioration of ecotoxic dyestuffs. The initial medium component screening for POX production was achieved using, One Factor at a Time and Placket-Burman methodologies with starch, casein and temperature as essential parameters. In auxiliary, Response Surface Methodology (RSM) was recruited and followed by model validation using Back propagation algorithm (BPA). RSM-BPA composite approach prophesied that combination of starch, casein, and temperature at optimal values 2.5%, 0.035% and 35 °C respectively, has resulted in 7 folds enhancement of POX outturn (2.52 U/mL) compared to the unoptimized media (0.36 U/mL). The concentrated enzyme decolorized 75.4% and 90% of the two azo dyes with lignin (10 mM), respectively. Hence, this investigation confirms the potentiality of mangrove actinomycete derived POX for elimination of noxious azo dyes to overcome their carcinogenic, mutagenic and teratogenic effects on humans and aquatic organisms.
AB - Peroxidase (POX) is a heme-containing oxidoreductase, its voluminous immuno-diagnostic and bioremediatory intuitions have incited optimization and large scale-generation from novel microbial repertoires. Azo dyes are the most detrimental classes of synthetic dyes and they are the common ecotoxic industrial pollutants in wastewater. In addition, azo dyes are refractory to degradation owing to their chemical nature, comprising of azoic linkages, amino moieties with recalcitrant traits. Moreover, they are major carcinogenic and mutagenic on humans and animals, whereby emphasizing the need for decolorization. In the present study, a novel POX from Streptomyces coelicolor strain SPR7 was investigated for the deterioration of ecotoxic dyestuffs. The initial medium component screening for POX production was achieved using, One Factor at a Time and Placket-Burman methodologies with starch, casein and temperature as essential parameters. In auxiliary, Response Surface Methodology (RSM) was recruited and followed by model validation using Back propagation algorithm (BPA). RSM-BPA composite approach prophesied that combination of starch, casein, and temperature at optimal values 2.5%, 0.035% and 35 °C respectively, has resulted in 7 folds enhancement of POX outturn (2.52 U/mL) compared to the unoptimized media (0.36 U/mL). The concentrated enzyme decolorized 75.4% and 90% of the two azo dyes with lignin (10 mM), respectively. Hence, this investigation confirms the potentiality of mangrove actinomycete derived POX for elimination of noxious azo dyes to overcome their carcinogenic, mutagenic and teratogenic effects on humans and aquatic organisms.
KW - Azo dyes
KW - Back propagation algorithm
KW - Computational docking
KW - Peroxidase
KW - Statistical modeling
KW - Streptomyces coelicolor
UR - https://www.scopus.com/pages/publications/85140069500
U2 - 10.1016/j.chemosphere.2022.136836
DO - 10.1016/j.chemosphere.2022.136836
M3 - Article
C2 - 36243089
AN - SCOPUS:85140069500
SN - 0045-6535
VL - 310
JO - Chemosphere
JF - Chemosphere
M1 - 136836
ER -