Purification and characterization of aspartic protease from Aspergillus niger and its efficient hydrolysis applications in soy protein degradation.

ABSTRACT:

Background

Adding 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.

Results

In 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, whi

SUBMITTER: Wei M 

PROVIDER: S-EPMC9983247 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature