Skip to Content
Merck
  • Change of the structure and the digestibility of myofibrillar proteins in Nanjing dry-cured duck during processing.

Change of the structure and the digestibility of myofibrillar proteins in Nanjing dry-cured duck during processing.

Journal of the science of food and agriculture (2017-12-08)
Xiaojing Du, Yangying Sun, Daodong Pan, Ying Wang, Changrong Ou, Jinxuan Cao
ABSTRACT

To investigate the change of bioavailability and structure of myofibrillar proteins during Nanjing dry-cured duck processing, carbonyl content, sulfhydryl (SH) group, disulfide (SS) group, sodium dodecyl sulfate polyacrylamide gel electrophoresis, surface hydrophobicity, secondary structures and in vitro digestibility were determined. During processing, carbonyl content and surface hydrophobicity increased; SH turned into SS group; α-helix turned into β-sheet and random coil fractions. Protein degradation occurred during dry-curing and drying-ripening stages. The in vitro digestibility of pepsin and pancreatic proteases increased during the salt curing stage and decreased during the drying-ripening stage. The increase of digestibility could be attributed to the mild oxidation, degradation and unfolding of proteins while the decrease of digestibility was related to the intensive oxidation and aggregation of proteins. Protein degradation was not a main factor of digestibility during the drying-ripening stage. Results demonstrated that the bioavailability loss of myofibrillar proteins in Nanjing dry-cured duck occurred during the stage of drying-ripening instead of curing. © 2017 Society of Chemical Industry.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Trypsin from porcine pancreas, lyophilized powder, Type II-S, 1,000-2,000 units/mg dry solid
Sigma-Aldrich
Pepsin from porcine gastric mucosa, powder, ≥400 units/mg protein
Sigma-Aldrich
α-Chymotrypsin from bovine pancreas, Type II, lyophilized powder, ≥40 units/mg protein