Functional Properties of Acetylated Chickpea Proteins

Abstract

Functional properties were investigated on chickpea proteins acetylated at 6 and 49% of the -amino groups of lysine. In water and in 0.25M NaCl solutions, acetylated chickpea proteins (ACP) were more soluble at high pH (pHϾ8), but less soluble at low pH (pH 2-7), than native chickpea protein (NCP). The solubility of ACP and NCP was reduced in 0.25-0.75M CaCl 2 solutions. Acetylation increased the water and oil absorption capacity of ACP. ACP also had higher emulsion capacity than that of NCP, but acetylation made emulsions of chickpea protein dispersions less stable.These improvements were attributed to the conformational changes in the protein molecules. The related changes in functionality are affected by the extent of acetylation. Extensive acetylation increased hydrophobicity of glycinin while moderately acetylated glycinin showed low hydrophobicity (Kim and Rhee, 1989). The viscosity of field bean and fat absorption of winged bean were related to the degree of acetylation (Schmidt and Schmandke, 1987, Narayana andNarasinga Rao, 1984). Barman et al. (1977) showed that the effect of acetylation could be predicted and the functional properties of soy protein could be altered by varying degrees of acetylation. Thus, acetylation provides a means of improving the functionality of chickpea proteins and may enable further understanding of their behavior in food systems. Our objective was to investigate the effects of acetylation on the functional properties of chickpea proteins.

Protein concentrate fromJatropha curcasscrew‐pressed seed cake and toxic and antinutritional factors in protein concentrate

“…This could possibly be due to the different nature of protein in Jatropha seed cake compared with that in Moringa seeds or other seeds for which higher solubility of proteins in NaCl has been reported in the literature. The results obtained in the present study are similar to those obtained by Bera and Mukherjee23 for rice bran proteins and by Liu and Hung24 for chickpea proteins. These authors showed decreased solubility in the presence of NaCl.…”

PHYSICOCHEMICAL AND PROCESSING FUNCTIONAL PROPERTIES OF PROTEINS FROM TWO CHINESE CHICKPEA (CICER ARIETINUML.) CULTIVARS

“…The ESI of the chickpea protein isolates was lowest at pH 4.0, and increased slightly when the pH was adjusted to a value higher than 4.0, but markedly increased at pH 3.0, which was similar to EAI at pH 3.0. This result was in agreement with those reported earlier for chickpea (Liu and Hung 1998b) and Dolichos lablab bean (Lawal 2005). Contrary to EAI, GCPI presented a lower ESI than ZCPI over a pH range of 4.0–8.0.…”

“…When the pH was above the isoelectric point, the emulsifying capacity of chickpea protein isolates increased with the enhancement of pH, and the difference magnitude corresponded to their solubility (Fig. 1), which is in agreement with those reported earlier for chickpea (Liu and Hung 1998b), soybean (Crenwelge et al. 1974) and beach pea (Chavan et al.…”

“…So far, some researchers have studied the functional properties of chickpea protein (Paredes‐López et al. 1991; Liu and Hung 1998a,b; Sánchez‐Vioque et al. 1999; Kaur and Singh 2007; Zhang et al.…”

Study of Acetylated Food Proteins by Raman Spectroscopy

“…I n the food industry, acetylation with acetic anhydrides, one of the most common chemical modifications used for proteins, has been shown to be a very powerful tool for improving the functional properties of many plant proteins, including soy protein (Franzen and Kinsella 1976a;Umeya and others 1981), leaf protein (Franzen and Kinsella 1976b), sunflower (Kabirrullah and Wills 1982), cottonseed (Rahma and Narasinga Rao 1983), winged bean (Narayana and Narasinga Rao 1984), oat (Ma 1984), faba bean (Muschiolik and others 1987;Krause and others 1996), rapeseed (Gruener and Ismond 1997), chickpea (Liu and Hung 1998), and mung bean (Ei-Adawy 2000).…”