The fluorescence of papain.

Biochim Biophys Acta

Published: March 1970

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http://dx.doi.org/10.1016/0005-2795(70)90123-6DOI Listing

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Effects of enzymolysis by seven proteases (Alcalase, Bromelain, Flavourzyme, Papain, Pepsin, Protamex, and Trypsin) with distinct cleavage specificities on the emulsification performance of hempseed protein (HPI) and its correlation with the structural and interfacial characteristics were explored in this study. Upon enzymolysis, a remarkable decrease in α-helix and β-turn was observed in resultant hydrolysates (HPH), accompanied by a rise in β-sheet and random coil, notably by Alcalase, Bromelain, Papain, and Trypsin. Overall, proteolysis led to noticeable reductions in surface hydrophobicity and total sulfhydryls as well as a redshift in intrinsic fluorescence, with Papain showing the most pronounced effects, possibly due to its higher hydrolysis degree (4.

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Article Synopsis
  • - The research focused on creating and analyzing acetylated starch/papain composites by using a specific method to encapsulate papain in acetylated cassava starch, with a low degree of substitution (DS = 0.037).
  • - Results showed that increasing starch concentration improved encapsulation efficiency (EE) but decreased loading capacity (LC) due to aggregation, while surfactants like Tween 80 enhanced EE and LC but reduced papain activity.
  • - The best results were found with a 30 mg/mL starch concentration, 7 mL solution volume, and 3% v/v Tween 80, achieving a high EE of 96.23% but lowering papain activity to 56%; however
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