Proteolytic Activity of Zingiber officinale Extract: Interaction With Myofibrillar Proteins of Different Origins and Functional Effects in Meat Systems.

Abstract

Plant-derived proteases are widely investigated as sustainable tools for meat tenderization; however, their efficacy depends on enzyme characteristics, concentration, and muscle origin. This study compared a crude Zingiber officinale extract with bromelain and papain, two of the most established plant proteases in the food industry, integrating kinetic analysis on isolated myofibrils with technological and sensory evaluation in marinated chicken breast (CB) and pork loin (PL). Proteolytic kinetics were assessed using CB-MF and PL-MF at increasing enzyme protein concentrations. Based on catalytic efficiency, the most active preparations (B-III, P-III, ZR-III) were selected for validation in whole muscle systems. Chicken myofibrils exhibited greater susceptibility to proteolysis than pork, while ginger extract showed substrate-dependent behavior with preferential activity toward CB-MF. Enzymatic marination increased myofibrillar fragmentation in both species without altering pH, confirming that structural modifications were enzyme-driven. Ginger treatment induced rapid early-stage fragmentation (6 h), whereas bromelain and papain promoted more extensive degradation at longer times (12 h). Cooking yield and water-holding capacity were primarily influenced by muscle type and marination time. Chicken consistently showed higher moisture retention than pork. Ginger extract promoted controlled proteolysis, preserving cooking performance relative to bromelain and papain. Sensory evaluation under optimal conditions (6 h) demonstrated enhanced juiciness, tenderness, flavor perception, and overall acceptability in ginger-treated samples, particularly in chicken. Overall, the integrated experimental evidence identifies ginger protease as a selective and moderate proteolytic system capable of enhancing meat quality while preventing excessive structural breakdown.