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Bioproduction, purification, partial characterization and phenol removal efficacy of tyrosinase enzyme from Streptomyces sp. strain MR28.
Rudrappa, Muthuraj; Santosh Kumar, M; Basavarajappa, Dhanyakumara Shivapoojar; Hiremath, Halaswamy; Hugar, Anil; Almansour, Abdulrahman I; Kantli, Gireesh Babu; Nayaka, Sreenivasa.
Affiliation
  • Rudrappa M; P.G. Department of Studies in Botany, Karnatak University, Dharwad, 580003, Karnataka, India. Electronic address: rmuthuraj20@gmail.com.
  • Santosh Kumar M; Department of Studies in Biochemistry, Davangere University, Davangere, 577007, Karnataka, India.
  • Basavarajappa DS; P.G. Department of Studies in Botany, Karnatak University, Dharwad, 580003, Karnataka, India.
  • Hiremath H; P.G. Department of Studies in Botany, Karnatak University, Dharwad, 580003, Karnataka, India.
  • Hugar A; P.G. Department of Studies in Botany, Karnatak University, Dharwad, 580003, Karnataka, India.
  • Almansour AI; Department of Chemistry, College of Science, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi Arabia.
  • Kantli GB; Department of Life Sciences, PIAS, Parul University, Vadodara, 391760, Gujarat, India.
  • Nayaka S; P.G. Department of Studies in Botany, Karnatak University, Dharwad, 580003, Karnataka, India. Electronic address: sreenivasankud@gmail.com.
Environ Res ; 251(Pt 2): 118701, 2024 Jun 15.
Article in En | MEDLINE | ID: mdl-38508362
ABSTRACT
The study focused on the production of the tyrosinase enzyme from Streptomyces sp. MR28 and its potency in removal of phenol content from water using free and immobilized tyrosinase enzyme. The tyrosinase was produced by Streptomyces sp. MR28 in liquid tyrosine broth medium, and it was further purified to near its homogeneity by employing, precipitation, dialysis, and column chromatography. After the purification, 44.49% yield with a 4 fold purification was achieved. The characterization of the purified enzyme showed a single major peak on HPLC and a solitary band on SDS-PAGE. The purified tyrosinase enzyme was active at a pH of 7.0 and a temperature of 30 °C. Further immobilization of purified tyrosinase was performed using the sodium alginate entrapment method. The capacity of the purified tyrosinase to remove phenol in water was evaluated by spectrophotometric method. The free tyrosinase enzyme-treated solutions showed a gradual decrease in the concentration of phenol with increased incubation time at 30 °C and 40 °C, at 90 min of the incubation time, it showed maximum efficacy in removing phenol from the solution. At 50 °C and 60 °C, the free tyrosinase enzyme exhibited very less capacity to remove the phenol. The immobilized enzyme showed good capacity for the removal of phenol from the solutions; the concentration of phenol in the solution decreased with an increase in the incubation time. At temperatures of 40 °C and 50 °C, the immobilized tyrosinase enzyme beads showed significant removal of phenol from the solution, and at temperatures of 30 °C and 60 °C, they also exhibited good capacity for the removal of phenol. At the end of the 90 min incubation period, it exhibited good capability. The current study suggests using immobilized microbial tyrosinase enzyme can be used for the removal of phenol from the contaminated water in a greener manner.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Streptomyces / Monophenol Monooxygenase / Phenol / Enzymes, Immobilized Language: En Journal: Environ Res Year: 2024 Document type: Article Country of publication: Países Bajos

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Streptomyces / Monophenol Monooxygenase / Phenol / Enzymes, Immobilized Language: En Journal: Environ Res Year: 2024 Document type: Article Country of publication: Países Bajos