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Identification of a Streptomyces sp. SCUT-3 aminopeptidase SsLap1 and its synergistic with endopeptidase Sep39 for peanut meal hydrolysis

文献类型： 外文期刊

作者： Cai, Hua-Hong 1 ; Zhang, Ming-Shu 1 ; Wu, Lei 1 ; Li, Zhi-Wei 1 ; Qin, Can 1 ; Liang, Chu-Yan 1 ; Deng, Jun-Jin 2 ; Luo, Xiao-Chun 1 ;

作者机构： 1.South China Univ Technol, Guangzhou Higher Educ Mega Ctr, Sch Biol & Biol Engn, Guangzhou 510006, Guangdong, Peoples R China

2.Guangdong Acad Agr Sci, Agrobiol Gene Res Ctr, State Key Lab Swine & Poultry Breeding Ind, Guangdong Prov Key Lab Crop Germplasm Resources Co, Guangzhou 510640, Peoples R China

关键词： Aminopeptidase; Multisite integration; Synergistic enzymolysis; Peanut meal; Debittering

期刊名称：FOOD BIOSCIENCE （ 影响因子：5.9； 五年影响因子：6.1 ）

ISSN： 2212-4292

年卷期： 2025 年 71 卷

页码：

收录情况： SCI

摘要： The persistence of bitter peptides in enzymatically hydrolyzed protein products remains a major organoleptic challenge in food biotechnology. In this study, the aminopeptidase SsLap1 from Streptomyces sp. SCUT-3 was successfully expressed in Pichia pastoris GS115. The recombinant SsLap1 exhibited exceptional catalytic efficiency with high specific activity (21,250.17 U/mg), excellent thermal stability (optimal temperature 65 degrees C, full activity retention after 2 h at 45-55 degrees C) and pH adaptability (optimal pH 8.0, stable in pH 7.0-9.0). SsLap1 exhibited the highest hydrolytic activity toward Leu-pNA. Notably, 1 mmol/L Co2+ and Ni2+ significantly enhanced its activity, reaching 582.07 % and 207.22 % of the control group, respectively. Furthermore, leveraging Phi C31 and Phi BT1 integrase modules, a multi-site integration system was constructed in Streptomyces sp. SCUT-3, enabling the high-efficiency co-overexpression of aminopeptidase SsLap1 and endopeptidase Sep39. This dual-enzyme system synergistically hydrolyzed peanut meal proteins, achieving 67.49 % and 34.51 % of total protein and amino acid recovery rate, which were 4.99 and 5.68-fold of wild-type treatment group. Critically, the system elevated free hydrophobic amino acids (e.g., 3.63-fold increase in Val) while reducing bitter peptide accumulation through SsLap1-mediated N-terminal residue cleavage. This enzyme preparation holds promising applications in the food industry, as it enhances the free amino acid content in protein hydrolysates while simultaneously reducing bitterness, thereby improving product flavor.

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