Abstract: Collagen was isolated from chicken feet by using papain and pepsin enzymes in acetic acid solution at 4°C for 24h with a yield of 18.16% and 22.94% by dry weight, respectively. Chemical composition and characteristics of chicken feet collagen such as amino acid composition, SDS-PAGE patterns, FTIR spectra and thermal properties were evaluated. The chicken feet collagen is rich in the amino acids glycine, glutamic acid, proline and hydroxyproline. Electrophoresis pattern demonstrated two distinct α-chains (α1 and α2) and β chain, indicating that type I collagen is a major component of chicken feet collagen. The thermal stability of collagen isolated by papain and pepsin revealed stable denaturation temperatures of 48.40 and 53.35°C, respectively. The FTIR spectra of both collagens were similar with amide regions in A, B, I, II and III. The study demonstrated that chicken feet collagen using papain isolation method is possible as commercial alternative ingredient.
Abstract: The present work represents an investigation of the
hydrolysis of hull-less pumpkin (Cucurbita Pepo L.) oil cake protein
isolate (PuOC PI) by pepsin. To examine the effectiveness and
suitability of pepsin towards PuOC PI the kinetic parameters for
pepsin on PuOC PI were determined and then, the hydrolysis process
was studied using Response Surface Methodology (RSM). The
hydrolysis was carried out at temperature of 30°C and pH 3.00. Time
and initial enzyme/substrate ratio (E/S) at three levels were selected
as the independent parameters. The degree of hydrolysis, DH, was
mesuared after 20, 30 and 40 minutes, at initial E/S of 0.7, 1 and 1.3
mA/mg proteins. Since the proposed second-order polynomial model
showed good fit with the experimental data (R2 = 0.9822), the
obtained mathematical model could be used for monitoring the
hydrolysis of PuOC PI by pepsin, under studied experimental
conditions, varying the time and initial E/S. To achieve the highest
value of DH (39.13 %), the obtained optimum conditions for time
and initial E/S were 30 min and 1.024 mA/mg proteins.