Reduce it to 50 words without loosing the meaning of the scientific text: The hydrolysis of proteins by bromelain is a complex enzymatic process that begins with the binding of bromelain's active site to specific peptide bonds in the protein. The cysteine residue in bromelain's active site then acts as a nucleophile, attacking the carbonyl group of the peptide bond and forming a temporary covalent intermediate. This attack leads to the cleavage of the peptide bond, effectively "cutting" the protein into smaller fragments. Once the bond is broken, bromelain releases these fragments and is free to repeat the process on other protein molecules. This continuous action results in the breakdown of large protein structures into smaller peptides and eventually individual amino acids. In meat, bromelain primarily targets structural proteins like collagen and elastin in connective tissues, as well as myofibrillar proteins such as actin and myosin. The gradual degradation of these proteins leads
Bromelain hydrolyzes proteins by binding to specific peptide bonds, with its cysteine residue acting as a nucleophile to cleave these bonds. This process breaks down large proteins, particularly collagen and elastin in meat, into smaller peptides and amino acids, allowing bromelain to continuously act on other protein molecules.