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Factors affecting thein vitro protein digestibility of chickpea albumins

✍ Scribed by Clemente, Alfonso; Vioque, Javier; S�nchez-Vioque, Ra�l; Pedroche, Justo; Bautista, Juan; Mill�n, Francisco

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
195 KB
Volume
80
Category
Article
ISSN
0022-5142

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✦ Synopsis

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 interand 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 signi®cant (P 0.05) increment in IVPD in the presence of b-ME, con®rming the essential role of disulphide bonds in stabilising the protein structure of the albumin fraction.

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