Optimization of Enzymatic Hydrolysis of Tilapia Scale Calcium Binding Peptides by Response Surface Methodology and Its Structural Characterization

HUANG Wen; YU Kenan; LIAO Wanwen; ZHONG Ruimin; CAO Yong; MIAO Jianyin

doi:10.13386/j.issn1002-0306.2021020099

Volume 42 Issue 21

Oct. 2021

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Science and Technology of Food Industry > 2021 > 42(21): 190-196. > DOI: 10.13386/j.issn1002-0306.2021020099

HUANG Wen, YU Kenan, LIAO Wanwen, et al. Optimization of Enzymatic Hydrolysis of Tilapia Scale Calcium Binding Peptides by Response Surface Methodology and Its Structural Characterization[J]. Science and Technology of Food Industry, 2021, 42(21): 190−196. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2021020099.

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Optimization of Enzymatic Hydrolysis of Tilapia Scale Calcium Binding Peptides by Response Surface Methodology and Its Structural Characterization

1.
College of Food Science, South China Agricultural University, Guangdong Provincial Key Laboratory of Nutraceuticals and Functional Foods, Guangzhou 510642, China
2.
College of Yingdong Food Science, Shaoguan University, Shaoguan 512005, China

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Received Date: February 17, 2021
Available Online: August 27, 2021

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Abstract

Abstract

In order to obtain the optimum enzyme hydrolysis conditions and chelating properties of tilapia scale calcium binding peptides, and provide basis for study of promoting calcium absorption of active material, in this study, the decalcified tilapia scales as raw material and calcium chelation activity as an index, papain was selected to optimize enzyme hydrolysis of the tilapia scales to obtain tilapia scale calcium binding peptides. The properties of the tilapia scale calcium binding peptides were characterized by amino acid analysis, ultraviolet-visible spectroscopy and fourier transform infrared spectroscopy. The optimal enzymatic hydrolysis conditions were as follows: the concentration of substrate 8%, time 2 h, enzyme to substrate ratio 0.3%, pH7 and temperature 60 ℃. Under these conditions, the calcium chelation activity of the enzymatic hydrolysate was (38.31±0.4) µg/mL. The results of characterization showed that, after chelating calcium, the contents of aspartic acid, glutamic acid, glycine, lysine, serine, cysteine and histidine in peptide-calcium chelate increased by 0.88%, 1.48%, 0.34%, 0.53%, 0.04%, 0.38% and 0.46%, respectively. The carboxyl oxygen and amino nitrogen groups in the calcium binding peptides participated in binding with calcium ions to form the tilapia scale peptide-calcium chelate. Tilapia scale calcium binding peptides has high calcium chelation activity, which lays a foundation for the production and application of calcium supplements.
- tilapia scales,
- enzymolysis,
- calcium binding peptides,
- structural characterization

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