• ASEP A. PRIHANTO Department of Fishery Product Technology, Faculty of Fisheries and Marine Science, Brawijaya University, Jl. Veteran Malang, East Java 65145, Indonesia
  • HAPPY NURSYAM Department of Fishery Product Technology, Faculty of Fisheries and Marine Science, Brawijaya University, Jl. Veteran Malang, East Java 65145, Indonesia
  • RAHMI NURDIANI Bioseafood Research Unit, Faculty of Fisheries and Marine Science, Brawijaya University, Jl. Veteran Malang, East Java 65145, Indonesia
  • HIDAYATUN MUYASYAROH Bioseafood Research Unit, Faculty of Fisheries and Marine Science, Brawijaya University, Jl. Veteran Malang, East Java 65145, Indonesia
  • ROYANI L. HAYATI Post Graduate Program, Brawijaya University, Jl. MT Haryono Malang, East Java 65145, Indonesia
  • ANIS MIFTACURROCHMAH Bioseafood Research Unit, Faculty of Fisheries and Marine Science, Brawijaya University, Jl. Veteran Malang, East Java 65145, Indonesia



Arthrospira platensis, Immune response, L-asparaginase, Modeling


Objective: This work aimed to study the modeling, binding site, and immunogenicity analysis of genes encoding L-asparaginase from Arthrospira platensis NIES 39.

Methods: Physicochemical characteristic of the gene was analyzed using ProtParam. I-TASSER, PROCHECK, ProSA, and ProQ were used to build the L-asparaginase model. The enzyme's binding site was achieved based on the SiteMap and COACH analysis. Immunogenicity analysis was based on MHC II binding epitopes on the immune epitope database with further epitope prediction, such as NN-align, SMM aligns, Combinatorial library, and Net MHCIIpan.

Results: The result showed that the protein had an aliphatic index of 94.46. It was dominated by strand, helix, and coil groups. The best template for building the model was the malonate-bound human L-asparaginase protein. The amino acid at 173,191,193, 201, 204, 205, 223, and 225 positions served as binding sites. The best substrate for A. platensis NIES 39 asparaginase was L-asparagine. There is no substantial evidence that the protein is highly allergenic.

Conclusion: In conclusion, this is the first report on the character of ASNase from microalgae A. platensis where the enzyme has the potential to be applied for health applications because of its low allergenicity.


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