Cloning, Expression, and Characterization of Novel Laccase Enzyme from NativeBacillussubtilisStrain OH67

Hajipour O., Dogan N. M., DİNÇER S., Norizadehazehkand M.

MOLECULAR BIOLOGY, vol.54, no.4, pp.611-617, 2020 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 54 Issue: 4
  • Publication Date: 2020
  • Doi Number: 10.1134/s0026893320040068
  • Journal Name: MOLECULAR BIOLOGY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, BIOSIS, CAB Abstracts, EMBASE, Veterinary Science Database
  • Page Numbers: pp.611-617
  • Çukurova University Affiliated: Yes

Abstract

Bacterial laccases are very stable at high temperature and high pH values, and have many biotechnological and industrial applications. Here we describe how we cloned, expressed and purified the laccase fromBacillus subtilis(B. subtilis).The enzyme molecular weight has been determined as 34 kDa in SDS- PAGE analysis. The activity of the recombinant enzyme has been proved by guaiacol oxidation. TheK(M)andV(max)values of the enzyme were at 1.1077 mM and at 19.3 mu mol/min/mg, respectively. The recombinant laccase was effective in the decolorization of Turquoise blue HF6, Remazol red 106, Remazol brilliant orange 3R, and Brilliant blue, thus, possessing the characteristics necessary for its possible application in textile and environmental industries.