• A change towards the secondary, tersier, dan quartener of protein
molecule without breaking the peptide bonds or a breakdown of the secondary and tersier protein because the breaking of hydrogen bond, hidrofobic interactions or disulfide bond where denaturation wont break the peptide bonds and the primer molecule structure wont be damage. • There are two types of denaturation that is protein breaking without developing peptide chain and the develop of peptide chain that will develop polipeptida • Denaturation causes the product to lose the enzim activity, solubility addition and dehydration and colour change and it can happen because heat treatment, pH, salt, and surface tension Positive and Negative side • Negative side: Protein loses its biological activity Protein deposition Protein loses its functional purpose • Positive side: Protein denaturation of heat in trypsin inhibits in legumes can increase he level of digestibility and biological avaibility of legume proteins Organic proteins are partially digestible, foam forming proteins and emulsions are better than natural proteins To make protein gel