Antityrosinase Mechanism and Antimelanogenic Effect of Arbutin Esters Synthesis Catalyzed by Whole-Cell Biocatalyst

  • J Agric Food Chem. 2021 Apr 14;69(14):4243-4252. doi: 10.1021/acs.jafc.0c07379.
Haixia Xu  1 ,  Xiaofeng Li  1 ,  Xuan Xin  1 ,  Lan Mo  1 ,  Yucong Zou  1 ,  Guanglei Zhao  2 ,  Yigang Yu  1 ,  Kebing Chen  3
Affiliations
  • 1. School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
  • 2. State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510641, China.
  • 3. Department of Spine Surgery, Center for Orthopaedic Surgery, The Third Affiliated Hospital of Southern Medical University, Academy of Orthopedics of Guangdong Province, Guangzhou 510630, China.
PMID: 33821640 DOI: 10.1021/acs.jafc.0c07379
Abstract

Tyrosinase is a key enzyme responsible for enzymatic browning of fruits and vegetables and skin disorders due to overproduction of melanin. Arbutin is an inhibitor of tyrosinase; however, its high polarity and weak transdermal absorption capacity limit its applications. In this paper, a green solvent system was developed to successfully synthesize arbutin esters with improved liposolubilities (Clog P values = 0.27-5.03). Among the obtained esters, arbutin undecenoate (AU) showed the strongest tyrosinase-inhibiting activity (15.6%), which was 9.0 times higher than that of arbutin. An enzyme kinetics study indicated that AU was a competitive inhibitor with reversible inhibition. The esters inhibited Tyrosinase by making the secondary structure of Tyrosinase looser and less stable; moreover, the interactions between Tyrosinase and AU driven by metal interactions and hydrogen bonds also offered a mechanism for inhibition of AU on Tyrosinase. In addition, AU (100 μM) reduced the melanin content of B16 mouse melanoma cells to 61.3% of the control group.

Keywords
antimelanogenic; biocatalysis; molecular docking; tyrosinase inhibition.
Products