Functional analysis and structure determination of alkaline protease from Aspergillus flavus

Abstract

Proteases are one of the highest value commercial enzymes as they have broad applications in food, pharmaceutical, detergent, and dairy industries and serve as vital tools in determination of structure of proteins and polypeptides. Multiple application of these enzymes stimulated interest to discover them with novel properties and considerable advancement of basic research into these enzymes. A broad understanding of the active site of the enzyme and of the mechanism of its inactivation is essential for delineating its structure-function relationship. Primary structure analysis of alkaline protease showed 42% of its content to be alpha helix making it stable for three dimensional structure modeling. Homology model of alkaline protease has been constructed using the X-ray structure (3F7O) as a template and swiss model as the workspace. The model was validated by ProSA, SAVES, PROCHECK, PROSAII and RMSD. The results showed the final refined model is reliable. It has 53% amino acid sequence identity with the template, 0.24 Å as RMSD and has -7.53 as Z-score, the Ramachandran plot analysis showed that conformations for 83.4 % of amino acid residues are within the most favored regions and only 0.4% in the disallowed regions.

Metabolomic Profiles of Aspergillus oryzae and Bacillus amyloliquefaciens During Rice Koji Fermentation

“…In addition to Aspergillus , the bacterial genus Bacillus is widely used for fermenting soybean meal. Bacillus is an ideal industrial microorganism because of its high growth rate and strong capacity to produce extracellular enzymes [10]. Bacillus subtilis yields compounds exhibiting various biological functions, and foods fermented by Bacillus spp.…”

Green recycling of chicken feather and sheep wool using the partially purified alkaline protease from <i>Bacillus circulans</i> L.

“…Proteases are hydrolytic enzymes that degrade protein into polypeptides, dipeptides and then to amino acids [1]. In particular, bacterial alkaline proteases play an important role in the industrial biotechnological processes and they are one of the highest value commercial enzymes as they have broad applications in food, pharmaceutical, detergent, and dairy industries [2]. Of them, Bacillus species are considered the most efficient for such purpose as they produce large quantities of the enzyme [3][4][5].…”

In silico characterization of broad range proteases produced by Serratia marcescens EGD‐HP20

“…The 3D model for the disulfide reductase showed least homology and only 14% query coverage and 21% sequence identity with the template c3iraA. The PROCHECK report which describes the stereo‐chemical quality for 3D structures revealed that Phyre2‐generated 3D protein structures of template displayed comparable structural homology with the reference proteins with well resolved crystallographic PDB structures as has also been displayed by SWISS‐MODEL, ProSA .…”