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.

从黑曲霉CICIM F0215 中鉴定并生化表征了一种新的氨肽酶 (An-APa) 。它在 40 °C 和 pH 7.0 时具有最大活性，并且对 N 端的亲水性和疏水性氨基酸残基表现出广泛的底物特异性。An-APa 水解 1 小时后，酪蛋白-胃蛋白酶和大豆分离蛋白 (SPI)-胃蛋白酶水解物同时释放亲水性和疏水性氨基酸，疏水性氨基酸具有Q显着释放大于 1500 cal/mol 的值（疏水度）。用 An-APa 处理后酪蛋白水解物中的 Leu、Ile、Phe、Tyr、Trp、Pro、Val 和 Lys 分别增加了 18.61、0.84、11.35、13.18、3.34、6.30、7.46 和 8.19 毫克/100 毫升SPI 水解物中的浓度分别为 19.72、1.47、18.37、11.72、4.61、4.10、8.13 和 5.85 mg/100 mL。两者分别占酪蛋白和 SPI 水解产物释放的游离氨基酸总量的 65.0% 和 64.4%。这表明 An-APa 可能适用于脱苦蛋白质水解产物。