Reduction of β-ODAP and IP6 contents in Lathyrus sativus L. seed by high hydrostatic pressure
Grass pea (Lathyrus sativus L.) seeds contain an endogenous neurotoxic non-proteinogenic amino acid, β-N-oxalyl-l-α,β-diaminopropionic acid (β-ODAP), a major limiting factor-for their human consumption. Furthermore, phytate (IP6), a well-known antinutrient is present in concentration capable of hindering bioavailability of iron (Fe), zinc (Zn), calcium (Ca), phosphorus (P) and other micronutrients from the seeds. Due to the reported capability of high hydrostatic pressure (HHP) to reduce the content of certain antinutritional/toxic agents in seeds and grains, the impact of HHP on the reduction of β-ODAP and IP6 were investigated. The contents of β-ODAP of accessions from different regions in Ethiopia were found to be in the range of 51.94 to 806.52 mg/100 g. Accession (GF1- Alemu, AK) exhibiting the highest β-ODAP content was selected for HHP treatment in soaked and batter forms using Central Composite Face Centered Design of experiments. The best HHP conditions in respect to β-ODAP reduction were also applied to the accession (GP-240038) with the lowest β-ODAP-content, a genetically improved variety (Wassie) and a variety from Germany (GR). The HHP treatment at 600 MPa for 25 min of seeds soaked for 6 h and 12 h exhibited the maximum reduction of β-ODAP (232.11 mg/100 g) and IP6 (21.11 mg/100 g) respectively. The combined incremental effect of pressure and soaking time resulted in a more significant (p ≤ .001) reduction in both compounds than the interaction of pressure with holding time (p ≤ .05). A reduction of β-ODAP from 36.00 to 71.22% by soaked-HHP treatment was observed. β-ODAP reductions were always higher for soaked compared to batter grass pea seeds. IP6 contents after HHP treatment ranged from 33.65 mg/100 g to nill. It can be concluded that pressure, soaking and holding time as well as the grass pea seed accession/variety had great impact on molecular structure changes, enhancement of enzyme activity and reduction in β-ODAP and IP6 content.
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