A novel aminopeptidase with potential debittering properties in casein and soybean protein hydrolysates
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A novel aminopeptidase with potential debittering properties in casein and soybean protein hydrolysates Peng Song1,2 • Lei Cheng1,2 • Kangming Tian2 • Meng Zhang2 • Suren Singh3 • Dandan Niu2 • Bernard Prior4 • Nokuthula Peace Mchunu5 • Zheng-Xiang Wang2
Received: 20 February 2020 / Revised: 7 August 2020 / Accepted: 18 August 2020 Ó The Korean Society of Food Science and Technology 2020
Abstract A new aminopeptidase (An-APa) was identified and biochemically characterized from Aspergillus niger CICIM F0215. It had maximal activity at 40 °C and pH 7.0 and exhibited a broad substrate specificity both on hydrophilic and hydrophobic amino acid residues at N-terminals. With An-APa hydrolysis for 1 h, the casein-pepsin and soybean protein isolates (SPI)-pepsin hydrolysates released both hydrophilic and hydrophobic amino acids and the hydrophobic amino acids having Q values (degree of hydrophobicity) greater than 1500 cal/mol were remarkably released. Leu, Ile, Phe, Tyr, Trp, Pro, Val and Lys in the casein hydrolysate after treatment with An-APa increased 18.61, 0.84, 11.35, 13.18, 3.34, 6.30, 7.46, and 8.19 mg/ 100 mL, respectively, and 19.72, 1.47, 18.37, 11.72, 4.61, 4.10, 8.13, and 5.85 mg/100 mL, respectively, in the SPI & Zheng-Xiang Wang [email protected] Peng Song [email protected]
hydrolysate. Both accounted for 65.0% and 64.4% of total released free amino acids from casein and SPI hydrolysates, respectively. This indicated that An-APa could be potentially applicable in debittering protein hydrolysates. Keywords Aspergillus niger Aminopeptidase Cloning Characterization Hydrolytic property Protein hydrolysates debittering
Introduction The functional and application characteristics of protein products from either animal (meat, milk, and fish) or plant (soy, legume, and cereal) sources are improved or 1
College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China
2
Department of Biological Chemical Engineering, College of Chemical Engineering and Materials Science, Tianjin University of Science and Technology, Tianjin 300457, China
3
Department of Biotechnology and Food Technology, Faculty of Applied Sciences, Durban University of Technology, P. O. Box 1334, Durban 4001, South Africa
4
Department of Microbiology, University of Stellenbosch, Private Bag X1, Matieland 7602, South Africa
5
Agricultural Research Council, Biotechnology Platform, Private Bag X5, Onderstepoort 0110, South Africa
Lei Cheng [email protected] Kangming Tian [email protected] Meng Zhang [email protected] Suren Singh [email protected] Dandan Niu [email protected] Bernard Prior [email protected] Nokuthula Peace Mchunu [email protected]
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expanded when modified by certain proteolytic enzymes (Saha and Hayashi, 2001). These protein hydrolysates have been reported to show better processing characteristics due to improved solubility, hygroscopicity, foaming potency, gelatinisation ability, modified emulsifying capacity and reduced viscosity (Kodera et al., 200
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