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KMID : 1007520200290111491
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Food Science and Biotechnology
2020 Volume.29 No. 11 p.1491 ~ p.1499
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A novel aminopeptidase with potential debittering properties in casein and soybean protein hydrolysates
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Song Peng
Cheng Lei
Tian Kangming
Zhang Meng
Singh Suren
Niu Dandan
Prior Bernard
Mchunu Nokuthula Peace
Wang Zheng-Xiang
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Abstract
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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.
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KEYWORD
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Aspergillus niger, Aminopeptidase, Cloning, Characterization, Hydrolytic property, Protein hydrolysates debittering
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