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Factors affecting the in vitro protein digestibility of chickpea albumins
Author(s) -
Clemente Alfonso,
Vioque Javier,
SánchezVioque Raúl,
Pedroche Justo,
Bautista Juan,
Millán Francisco
Publication year - 2000
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/(sici)1097-0010(20000101)80:1<79::aid-jsfa487>3.0.co;2-4
Subject(s) - trypsin , albumin , chemistry , in vitro , trypsin inhibitor , digestion (alchemy) , fraction (chemistry) , biochemistry , intramolecular force , chromatography , food science , enzyme , stereochemistry
In vitro protein digestibility (IVPD) of chickpea albumins and its possible relationship to their structure and the presence of trypsin inhibitor activity (TIA) have been studied. Trypsin digestion of the albumin fraction under non‐reducing conditions was incomplete, while the reduction of inter‐ and intramolecular disulphide bonds caused an improvement in the accessibility of sites susceptible to trypsin digestion. Trypsin inhibitor activity in the chickpea albumin fraction was dependent upon both temperature and heating time. Although heating the albumin fraction at 100 °C for 30 min reduced the TIA by more than 50% with respect to the initial activity, an important TIA rate was attributable to heat‐resistant trypsin inhibitor. The TIA decrease was not related to an increase in the rate of IVPD. However, we observed a significant ( P ≤ 0.05) increment in IVPD in the presence of β‐ME, confirming the essential role of disulphide bonds in stabilising the protein structure of the albumin fraction. © 2000 Society of Chemical Industry