ArticleMicrobial cell factories2023
Purification and characterization of aspartic protease from Aspergillus niger and its efficient hydrolysis applications in soy protein degradation.
Article in Microbial cell factories, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Postbiotics at the interface of microbial biotechnology and therapeutics: industrial production, functional mechanisms, and clinical potentials.Archives of microbiology · 2026Review
- Liquid Microbial-Enzymatic Co-Fermentation of Walnut and Sesame Meals and Its Effects on Nutrient Digestibility in Growing Pigs.Animals : an open access journal from MDPI · 2026Article
- Special Characterization and Excellent Antioxidant Capabilities of Zinc Chelated Squid Protein Nanoparticles.Foods (Basel, Switzerland) · 2025Article
- Characterization of a novel aspartic protease from Trichoderma asperellum for the preparation of duck blood peptides.Applied microbiology and biotechnology · 2024Article
- Review
- Degradation and mechanism analysis of protein macromolecules by functional bacteria in tobacco leaves.Frontiers in microbiology · 2024Article
- Microbial-derived salt-tolerant proteases and their applications in high-salt traditional soybean fermented foods: a review.Bioresources and bioprocessing · 2023Review
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundAdding acid protease to feed can enhance protein digestibility, boost feed utilization, and stimulate the growth of animals in breading industry. In order to obtain an acid protease with high hydrolysis efficiency to plant protein, in this study, an aspartic protease from Aspergillus niger was heterologous expressed in Pichia pastoris (P. pastoris). The enzymatic properties and application in soybean protein degradation were also studied.
resultsIn our investigation, the high aspartic protease (Apa1) activity level of 1500 U/mL was achieved in 3 L bioreactor. After dialysis and anion exchange chromatography, the total enzyme activity and specific enzyme activity were 9412 U and 4852 U/mg, respectively. The molecular weight of the purified protease was 50 kDa, while the optimal pH and temperature were 3.0 and 50 °C, respectively. It was stable at pH 2.0-5.0 and 30-60 °C. Apa1 was used to hydrolyze soybean isolate protein (SPI) at 40 °C and pH 3.0, and a high hydrolysis degree (DH) of 61.65% was achieved. In addition, the molecular weight distribution of SPI hydrolysis products was studied, the result showed that the hydrolysis products were primarily oligopeptides with molecular weights of 189 Da or below.
conclusionsIn this study, Apa1 was successfully expressed in P. pastoris and high expression level was obtained. In addition, the highest protein hydrolysis rate to SPI degradation so far was achieved. The acid protease in this study provides a new protease that is suitable for the feed industry, which will be very helpful to improve the feed utilization and promote the development of the breeding industry.
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