Characterization of Flavor Properties from Fish (Collichthys niveatus) Through Enzymatic Hydrolysis and the Maillard Reaction. Issue 4 (18th May 2016)

• Record Type: Journal Article
• Authors: Zhao, Qiaoling; Shen, Qing; Guo, Rui; Wu, Jiajia; Dai, Zhi-yuan
• Is Part Of: Journal of aquatic food product technology. Volume 25:Issue 4(2016)
• Page Start: 482
• Page End: 495
• Publication Date: 2016-05-18
• Subjects: Volatile profile -- Maillard reaction -- enzymatic hydrolysis -- Collichthys niveatus -- gas chromatography mass spectrometry; Fishery processing -- Periodicals; Animal products -- Periodicals; Plant products -- Periodicals; 664.9405
• DOI: 10.1080/10498850.2013.873965
• Languages: English
• ISSNs: 1049-8850

Abstract

ABSTRACT: Collichthys niveatus ( C. niveatus ) is an abundant but underutilized fish species caught in China. In this study, flavor properties of the Maillard reaction products (MRPs) obtained from C. niveatus protein hydrolysates were determined. The optimized fish protein hydrolysates were prepared using commercial Alcalase, and the optimum values of temperature, pH, and enzyme/substrate ratio were 55.6°C, 8.7, and 1.03%, respectively. In addition, the volatile compounds of the MRPs were evaluated using headspace solid–phase microextraction combined with gas chromatography mass spectrometry. A total of 80 volatile compounds were separated and identified. Priazines, alcohols, and aldehydes were the major flavor contributors to the aroma of the MRPs (accounting for 38.86, 9.21, and 8.23%, respectively), while pyrazines were the most abundant group of volatile compounds present, with 2, 5-dimethyl-pyrazine, methylpyrazine, and 3-ethyl-2, 5-dimethylpyrazine being found in highest quantities (19.83, 5.81, and 5.70%, respectively). Other components—including alcohols, aldehydes, furans, ketones, and esters—were also identified in the MRPs. This study provides a systematic strategy for marine products processing and volatiles characterization. The results point to the information in the volatiles from the MRPs of protein hydrolysis from C. niveatus and pave the way for full utilization of this species.