Abstract:In order to study the structural characteristics of all Aspergillus-derived α-L-rhamnosidase, 300 non-repeated Aspergillus derived α-L-rhamnosidase nucleic acid sequences were collected using NCBI database and 21 of them were selected through evolutionary tree selection. Through sequence alignment analysis, the 21 sequences are independently and reliably representative. Using bioinformatics tools to analyze the physical and chemical properties, transmembrane region, and signal peptide, it was found that the isoelectric point (pI) of α-L-rhamnosidase derived from Aspergillus species was 4.66 to 7.17, and the number of amino acids, molecular weight and total number of atoms fluctuates greatly. Ten sequences have signal peptide sequences, 1 sequence is twice transmembrane protein, and 21 sequences are all hydrophilic proteins. The phylogenetic tree construction, three-level structure modeling and structure superposition show that these 21 representative sequences can be divided into two types. The first type contains one (α/α)6 barrel structure and one β sheet structure at the bottom of the barrel, and can be further divided into 4 sub-categories according to the number of additional β sheets contained; The second type has one (α/β)8 structure and β sheet structure surrounding the barrel structure domain. It elucidates the protein structure characteristics of α-L-rhamnosidase derived from Aspergillus, which helps to better clarify the common law of α-L-rhamnosidase and provide theoretical guidance for the modification of this enzyme.
