AI Article Synopsis
- The Aspergillus niger AS3.350 protease gene (pepD) was cloned and expressed in Pichia pastoris KM71, achieving an enzyme activity of 331.5 U/ml at optimal conditions of 45 °C and pH 8-9.
- Enzyme activity was inhibited by various compounds like PMSF and metal ions, but stimulated by calcium, which is crucial for rPepD expression and function.
- rPepD demonstrated a broad substrate range, showing effective hydrolysis of soy protein isolate, corn flour, and gluten meal, suggesting its potential use in food processing applications.
Article Abstract
The Aspergillus niger AS3.350 protease gene (pepD) was successfully cloned and expressed in Pichia pastoris KM71. The rPepD activity was 331.5 U/ml, and the optimum temperature and pH were 45 °C and 8-9 respectively. In addition, enzyme activity was significantly inhibited by PMSF, EDTA, Mg, Fe and Zn ions, and stimulated by Ca which selectively bound to the T and D residues. Mutation in either or both of the residues inhibited rPepD expression, indicating that binding to Ca is necessary for PepD expression and activity. The rPepD showed a wide substrate range, and was particularly selective to those with hydrophobic amino acids. The degree of rPepD-mediated hydrolysis of soy protein isolate, corn flour and gluten meal were 8.7%, 38.1% and 33.6% respectively, which was higher than that by Alcalase, indicating that rPepD has potential applications in the food processing industry.
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| http://dx.doi.org/10.1016/j.pep.2019.06.002 | DOI Listing |
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