## 3 Results and Discussion
### Amino Acid Profile  
The analysis revealed a greater level of amino acids in the LPC fractions than in the flour fractions (Table 2). This observation reinforces the hypothesis that the extraction process contributes to a more concentrated protein and a more comprehensive removal of non-protein constituents, yielding superior purity protein fractions. These findings also indicate that the glutelin fractions of flour and LPC exhibited higher hydrophobic amino acid, aromatic amino acid, negatively charged amino acid, branch chain amino acid, and total amino acid (TAA) levels. The most abundant amino acids in these fractions were leucine, valine, and glutamic acid. The amino acid profile differs from that of the protein fractions of _Amarant thus dubis_ leaves, with albumin being the most abundant fraction and containing high levels of aspartic acid, glutamine, and arginine [23]. This variation can be attributed to the composition of the foliar materials. Moreover, the glutelin fractions in this study contained higher levels of hydrophobic amino acids compared to the protein concentrate of the green biomass _Azolla pinnata_ fern (38.9 g/100 g). Higher levels of hydrophobic amino acids provide favourable surface active properties, such as emulsification and oil-binding properties [10]. Surface-active biopolymers must undergo migration, adsorption, and integration at the oil-water interface to decrease the interfacial tension. This process facilitates the positioning of hydrophobic amino acids toward the oil phase and hydrophilic moieties toward the aqueous phase [24]. Interestingly, the albumin fractions presented a greater TAA than the prolamin and globulin fractions. The prolamin fractions had low amino acid levels, and in the globulin fractions, no amino acids were detected despite their protein content being higher than that of the albumin fractions (Figure 1). The low detection or absence of amino acids, especially in the flour fractions, may result from impurities that hinder effective hydrolysis during sample processing. The incomplete recovery of amino acids could be ascribed to specific amino acids not being completely hydrolysed [25]. As a result, some amino acids produce multiple forms of _tert_-butyl dimethylsilyl (TBDMS) derivatives or incomplete derivatisation and interfere with the quantification [26]. This finding highlights the necessity for additional purification steps for globulin and prolamin fractions, indicating their limited suitability for food processing technologies in their current form. Likewise, the protein fractions did not contain lysine, arginine, histidine, and methionine. The absence of these amino acids may be attributed to the racemisation of amino acids or reactions of side chains with other components during prolonged exposure to hot acid [25]. Nonetheless, the amino acid compositions of the glutelin fractions of flour and LPC were superior to those of the other fractions. In fact, the glutelin fractions contained five essential amino acids, including valine, leucine, isoleucine, phenylalanine, and tyrosine. These essential amino acids met the recommended levels outlined by the WHO/FAO (2007) for adults [27]. In contrast, the albumin and prolamin fractions presented insufficient levels of essential amino acids. Unexpectedly, the glutelin fractions (flour and LPC) displayed a higher total amino acid (TAA) content than did the protein hydrolyses obtained by enzymatic hydrolysis with pepsin (37.4 g) and pancreatin (43.8 g) in previous investigations [18]. Notably, the protein hydrolyses did not contain tyrosine. In contrast, the glutelin protein