Because　of　the　health　benefits　and　economic　opportunities,　extracting　bioactive　peptides　from　plant　proteins,　often　food　processing　by-products,　garners　significant　interest.　However,　the　high　enzyme　costs　and　the　emergence　of　bitter　peptides　have　posed　significant　challenges　in　production.　This　study　achieved　the　immobilization　of　Alcalase　and　Flavorzyme　using　cost-effective　SiO2　microparticles.　Mussel-inspired　chemistry　and　biocompatible　polymers　were　employed,　with　genipin　replacing　glutaraldehyde　for　safer　crosslinking.　This　approach　yielded　an　enzyme　loading　capacity　of　approximately　25　mg/g　support,　with　specific　activity　levels　reaching　around　180　U/mg　for　immobilized　Alcalase　(IA)　and　35　U/mg　for　immobilized　Flavorzyme　(IF).　These　immobilized　proteases　exhibited　improved　activity　and　stability　across　a　broader　pH　and　temperature　range.　During　the　hydrolysis　of　soy　proteins,　the　use　of　immobilized　proteases　avoided　the　thermal　inactivation　step,　resulting　in　fewer　peptide　aggregates.　Moreover,　this　study　applied　peptidomics　and　bioinformatics　to　profile　peptides　in　each　hydrolysate　and　identify　bioactive　ones.　Cascade　hydrolysis　with　IA　and　IF　reduced　the　presence　of　bitter　peptides　by　approximately　20%.　Additionally,　50%　of　the　identified　peptides　were　predicted　to　have　bioactive　properties　after　in　silico　digestion　simulation.　This　work　offers　a　cost-effective　way　of　generating　bioactive　peptides　from　soy　proteins　with　reducing　potential　bitterness.