Purification and structure analysis of zinc-binding protein from Mizuhopecten yessoensis.

Abstract

Zn-binding protein was obtained after purification from scallops (Mizuhopecten yessoensis) using gel permeation and ion-exchange chromatography. Amino acid determination showed that the cysteine of the zinc-binding protein accounted for one-third of the total amino acids, which is a typical feature of metallothionein (MT). The spectra of Fourier Transform Infrared Spectroscopy (FTIR) and Circular Dichroism (CD) were analyzed to predict the secondary structure information of zinc-binding protein: the α-helix was 46.55%, the β-sheets was 27.07%, the random coil was 16.48%, and the β-turns was 9.89%. Using a commercial kit to measure its antioxidant activity in vitro, the result showed that it had good scavenging ability to 1,1-diphenyl-2-picrylhydrazyl (DPPH), hydroxyl radical (·OH), and reducing the ability to ferrous iron ions. With the process provided by this study, zinc-binding protein can be prepared in large quantities, which is the basis for its future commercialization. PRACTICAL APPLICATIONS: According to the extraction and purification process established in this study, a large amount of zinc-bound MT from the viscera of scallops can be obtained. And the zinc-bound MT had good antioxidant activity. In addition, the yield of each purification step has been calculated. The zinc-bound MTs from scallop' viscera can be prepared in large quantities by directly using the process in this manuscript or by equal magnification of this process. In the future, large-scale production can be considered to increase the economic value of scallops' viscera.