Β-galactosidases (bGALs) are a subgroup of glycoside hydrolase enzymes that play essential roles in plant growth and development, particularly in cell wall remodeling during fruit ripening. They catalyze the hydrolysis of β-D-galactosyl residues from polysaccharides, glycoproteins, and glycolipids, contributing to the softening of fruit tissue and changes in texture. This study aimed to identify and characterize the β-galactosidases gene family in mango (Mangifera indica) using a bioinformatics approach. A total of 18 MibGAL genes were identified through BLASTP searches against the Mangobase genome database. The physicochemical properties of the encoded proteins were analyzed using the ExPASy ProtParam tool. Conserved motifs were detected using MEME Suite, revealing shared structural features across most family members. Three-dimensional protein models were constructed using Phyre2, which showed a largely conserved folding pattern typical of ‘glycoside hydrolase 35’ enzymes, with some variation indicating potential functional divergence. The findings provide the first comprehensive overview of bGAL genes in mango and establish a foundational resource for future studies on fruit softening, postharvest biology, and genetic improvement of fruit quality traits.

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Survey of the β-galactosidase Gene Family in Mango (Mangifera indica): Genome-Wide Identification, Structural Characterization, and Motif Analysis

  • Toan Van Nguyen,
  • Hong Viet La,
  • Ha Duc Chu,
  • Phi Bang Cao

摘要

Β-galactosidases (bGALs) are a subgroup of glycoside hydrolase enzymes that play essential roles in plant growth and development, particularly in cell wall remodeling during fruit ripening. They catalyze the hydrolysis of β-D-galactosyl residues from polysaccharides, glycoproteins, and glycolipids, contributing to the softening of fruit tissue and changes in texture. This study aimed to identify and characterize the β-galactosidases gene family in mango (Mangifera indica) using a bioinformatics approach. A total of 18 MibGAL genes were identified through BLASTP searches against the Mangobase genome database. The physicochemical properties of the encoded proteins were analyzed using the ExPASy ProtParam tool. Conserved motifs were detected using MEME Suite, revealing shared structural features across most family members. Three-dimensional protein models were constructed using Phyre2, which showed a largely conserved folding pattern typical of ‘glycoside hydrolase 35’ enzymes, with some variation indicating potential functional divergence. The findings provide the first comprehensive overview of bGAL genes in mango and establish a foundational resource for future studies on fruit softening, postharvest biology, and genetic improvement of fruit quality traits.