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A novel neutral protease from a newly isolated and identified bacteria Enterobacter sp. NRCM1 was used to produce the enzymatic hydrolyzed soybean protein isolate (E-SPM1). The protease was purified and biochemically characterized. The effect of hydrolysis time on degree of protein hydrolysis and released free amino acids was investigated. The enzymatic hydrolysates (E-SPM124, E-SPM148 and E-SPM172) produced after 24, 48 and 72 h, respectively were used as main precursors of beef-like flavours. The generated volatiles were determined by solid phase microextraction combined with gas chromatography- mass spectrophotometer (SPME- GC-MS). The results revealed that the optimum pH and temperature of protease activity were 7.0 and 50oC, respectively. Sample E-SPM172 showed the highest degree of hydrolysis (43.71%) and content of free amino acids (5.78 g/mL). The headspace volatiles of the model mixture based on E-SPMI72 comprised the highest content of the most important compounds for meat aroma. The results of odour sensory analysis confirmed those of GC-MS for all investigated samples. The highest score of beefy note of sample E-SPMI72was mainly correlated to the significant increase of 2-methyl-3-furanthiol, the most potent aroma compound in beef flavour. The gradual increase of savoury note was consistent with that of the disulfide compounds, which possess savoury aromatic note.

egyptian journal of chemistry

Production of enzymatically hydrolyzed soybean protein isolate by a novel neutral protease from Enterobacter sp. NRCM1 to be used as a base precursor of thermal process flavours