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A novel aminopeptidase with potential debittering properties in casein and soybean protein hydrolysates

Food Science and Biotechnology 2020년 29권 11호 p.1491 ~ 1499
Song Peng, Cheng Lei, Tian Kangming, Zhang Meng, Singh Suren, Niu Dandan, Prior Bernard, Mchunu Nokuthula Peace, Wang Zheng-Xiang,
소속 상세정보
 ( Song Peng ) - Tianjin University of Science and Technology College of Biotechnology
 ( Cheng Lei ) - Tianjin University of Science and Technology College of Biotechnology
 ( Tian Kangming ) - Tianjin University of Science and Technology College of Chemical Engineering and Material Sciences Department of Biological Chemical Engineering
 ( Zhang Meng ) - Tianjin University of Science and Technology College of Chemical Engineering and Material Sciences Department of Biological Chemical Engineering
 ( Singh Suren ) - Durban University of Technology Faculty of Applied Sciences Department of Biotechnology & Food Technology
 ( Niu Dandan ) - Tianjin University of Science and Technology College of Chemical Engineering and Material Sciences Department of Biological Chemical Engineering
 ( Prior Bernard ) - University of Stellenbosch Department of Microbiology
 ( Mchunu Nokuthula Peace ) - Agricultural Research Council Biotechnology Platform
 ( Wang Zheng-Xiang ) - Tianjin University of Science and Technology College of Chemical Engineering and Material Sciences Department of Biological Chemical Engineering

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 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.

키워드

Aspergillus niger; Aminopeptidase; Cloning; Characterization; Hydrolytic property; Protein hydrolysates debittering

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