Abstract

Isolation of wound healing compounds from Heliotropium indicumDodehe Yeo, Barthélémy Attioua, Christine Lehalle, Metowogo Kossi, Jean David N’guessan, Allico Joseph Djaman, Annelise Lobstein, Nelly Frossard

Highlights

  • Tyrosinase (EC 1.14.18.1, monophenol, O-diphenol: oxygen oxidoreductase) is a copper-metalloprotein that is ubiquitously dispensed in nature

  • Described criteria were used for this study: identification to the species level was defined as >99% identity of the 16S ribosomal ribonucleic acid (rRNA) gene sequence with the sequence of its closest bacterial relative in the GenBank database, and identification at the genus level was defined as >99% identity of the 16S rRNA gene sequence with the sequence of its closest bacterial relative in the GenBank database (Sambrook et al, 1989)

  • This result was in good agreement with those obtained by Hullo et al (2001) who isolated and studied tyrosinase from B. subtilis

Read more

Summary

Introduction

Tyrosinase (EC 1.14.18.1, monophenol, O-diphenol: oxygen oxidoreductase) is a copper-metalloprotein that is ubiquitously dispensed in nature. Tyrosinase is a bifunctional enzyme and a monooxygenase that catalyzes the O-hydroxylation and subsequent oxidation of monophenols, O-phenols, to quinones (Claus and Decker 2006). Tyrosinase plays an important role in wound healing and the primary immune response of plant life, sponges and many invertebrate (Danial et al, 2018; Decker and Tuczek 2000). It is necessary to synthesize phenolic polymers such as tannins, lignin, and flavonoids. In fungi, this enzyme has crucial importance in virulence and survives reproductive organ differentiation, protection of tissue after infection and spore

Methods
Results
Conclusion
Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.