BIOCHEMICAL COMPOSITION AND PROTEOLYTIC ACTIVITY OF Cymbopogon Citratus PROTEASE

Abstract

Cymbopogon citratus has been identified as a source of protease inhibitors, yet the presence of proteases in it has often been overlooked. This study aimed to (i) analyze the biochemical composition of Cymbopogon citratus and (ii) evaluate the effectiveness of its proteolytic activity in degrading muscle proteins, providing insights into its potential applications. The stumps and leaves of the plant were extracted for oil, from which biochemical components were analyzed using Gas Chromatography (GC-MS). Furthermore, the effectiveness of the protease was measured using SDS-PAGE and Scanning Electron Microscopy (SEM). Stumps had higher aldehyde-ketone (88.57%) and hydrocarbon terpene (38.83%) contents compared to leaves (81.24% and 36.80%, respectively), while leaves had more alcohols (55.93% vs 45.84%). Stump protease degraded goat meat proteins in the 10-28 kDa range, including troponin C, troponin I, myosin heavy chain, and filamin (143-250 kDa). Leaf protease targeted proteins in a narrower 10-15 kDa range in both goat and beef samples. SEM revealed significant impacts on the extracellular matrix structure: stump protease predominantly affected endomysium, while leaf protease altered perimysium. These findings highlight the potential for enzymatic differentiation in meat tenderization, enabling targeted applications in the industry without compromising essential protein quality.