Enzymatic Degradation

Enzymatic degradation of food lipids produces free fatty acids that give rancid, soapy, cardboardy off-flavors, also as acidification of the food. Food texture is additionally altered. Lipolytic species mostly occur in Candida, Cryptococcus, Geotrichum, and Rhodotorula, and are implicated within the breakdown of fats in dairy and meat products, and in vegetable oil . Notable lipolytic species include Y. lipolytica, Cr. diffluens, C. zeylanoides, Cr. albidus, and Cr. laurentiiEnzymatic degradation studies were administered to demonstrate HyalSx metabolic resistance compared with heparin which is quickly degraded within the organism by heparinase [6]. The evaluation of the enzymatic digestion was estabilished by digestion of the compounds with Streptomyces hyalyronidase and analysis of the obtained fractions with SDS-Gel Electrophoresis. The not digested Hyal showed a characteristic wide band which disappeared when the digestion products were eluted with the solvent. On the contrary, the results obtained on HyalS3,3.5,4, demonstrated that hyaluronidase didn't digest these samples since the bands obtained are often superimposed upon the not digested Hyal band. These results were confirmed by Fast Flow Chromatography analysis. Infact, as shown in Fig. 8, the elution profile of Hyal changed due to enzymatic digestion, whereas HyalSx didn't change before and after treatment with the enzyme. The presence of charged sulphate groups determined the non attack of the enzyme.The adsorption of PHA depolymerase to P(3HB) single crystals has been investigated using immunogold labeling techniques.204,205 it's been found that PHA depolymerase adsorbed homogeneously on the surfaces of single crystals without site specificity. PHA depolymerases are inactive toward rubbery amorphous polyesters like native amorphous PHA granules and chemosynthetic atactic P(3HB).210 However, when amorphous P(3HB) was blended with crystalline P(3HB) or other crystalline polyesters, the enzymatic erosion was induced.210–212 These results suggest that the PHA depolymerase is susceptible to adsorb to stable crystalline lamellae, but it hardly binds to mobile polymer chains in an amorphous state