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The Potential Use of Fermented Chickpea and Faba Bean Flour as Food Ingredients.

Maria V Chandra-HioeChristina H M WongJayashree Arcot
Published in: Plant foods for human nutrition (Dordrecht, Netherlands) (2017)
Apart from being a rich and inexpensive protein source, legumes provide essential vitamins, minerals and dietary fibre. Considering the nutritional benefits, legumes flour can potentially be incorporated in the development of new products. The aim of this study was to investigate whether fermentation affects the protein content, in vitro protein digestibility, trypsin inhibitor activity and the functionality of proteins in faba bean, desi and kabuli chickpea. Australian grown chickpea and faba bean were selected and initially soaked, de-hulled, dried and milled into flour. This was fermented with lyophilised yoghurt cultures in a 30 °C orbital shaker for 16 h. While protein contents in fermented desi and kabuli flour were lower than their raw counterparts (p > 0.05), it was significantly higher in fermented faba bean. A significant increase (9.5%) in in vitro protein digestibility was found in fermented desi. Trypsin inhibitor activity in fermented desi, kabuli and faba bean reduced by 2.7, 1.1 and 4.7%, respectively (p > 0.05). Overall, the in vitro protein digestibility in flour samples increased, while simultaneously reducing the trypsin inhibitor activity. The water absorption capacity of the fermented kabuli flour significantly increased by 11.3%. All fermented flour samples had significantly higher oil absorption capacity than their corresponding raw flour that was likely due to increased insoluble hydrophobic protein. Although, the foaming capacity in all fermented flour samples was significantly lower than their respective raw samples, only fermented desi and faba bean flour showed lower foaming stability (p > 0.05). The present study suggests that fermented legume flour could fulfill the demand for innovative products of higher nutritional value.
Keyphrases
  • lactic acid
  • protein protein
  • binding protein
  • climate change
  • small molecule
  • water soluble