Tyrosinase Inhibitory and Antioxidant Activity of Enzymatic Protein Hydrolysate from Jellyfish (Lobonema smithii).

Maytamart Upata,Suthasinee Yarnpakdee,Sutee Wangtueai,Thanyaporn Siriwoharn,Joe M Regenstein,Sakunkhun Makkhun

doi:10.3390/foods11040615

Abstract

The optimization of antioxidant and anti-tyrosinase activity during jellyfish hydrolysate preparation was studied using a response surface methodology (RSM) with a face-centered composite design. The influence of the hydrolysis duration and the enzyme concentration on the IC50 of the DPPH and ABTS radical scavenging activity, ferric-reducing antioxidant power (FRAP), the degree of hydrolysis (DH), yield, and the IC50 value of tyrosinase inhibitory activity were determined. The optimum conditions for the production of jellyfish hydrolysate using alcalase (JFAH), flavourzyme (JFFH), or papain (JFPH) were achieved at hydrolysis times of 360, 345, or 360 min, respectively, and at an enzyme concentration of 5.0%. JFFH had the highest antioxidant and tyrosinase inhibitory activity. JFAH, JFFH, and JFPH concentrations of 2.5 mg/mL resulted in HaCaT cells (IC80) having a survival rate of 80%. The amino acid profile of JFFH contained about 43% hydrophobic and 57% hydrophilic amino acids, comprising Gly, Cys, Glx, Asx, which were dominant. The isolation of a peptide fraction from JFFH was carried out using ultrafiltration membranes (10, 3, and 1 kDa) and gel filtration chromatography. Fraction-III (1–3 kDa) showed the highest antioxidative and tyrosinase inhibitory activity.

Highlights

Tyrosinase, a copper-containing molecule, is an essential enzyme in melanin formation that accelerates the generation of melanin from tyrosine via oxidation
Tyrosinase activity is necessary for the provision of melanosomes into keratinocytes, and melanogenesis modulators can directly affect this activity [2]
The composition of the jellyfish tissue was largely determined based on the bodies of water in which these invertebrates were discovered

Summary

Introduction

Tyrosinase, a copper-containing molecule, is an essential enzyme in melanin formation that accelerates the generation of melanin from tyrosine via oxidation. The enzyme is predominantly involved in two melanin production reactions, i.e., the monophenolase reaction involving the hydroxylation of tyrosine and the diphenolase reaction for the oxidation of 3,4-dihydroxyl-L-phenylalanine (L-DOPA) to dopaquinone [1]. Tyrosinase activity is necessary for the provision of melanosomes into keratinocytes, and melanogenesis modulators can directly affect this activity [2]. Limiting tyrosinase activity in cosmetics and medicine can prevent the browning of foods and melanin synthesis [3]. The development and screening of tyrosinase inhibitors to be used as cosmetics products and food additives has been of interest in the industrial sector [4,5,6]

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Methods

Results