Physicochemical and Organoleptic Characteristics of Seasoning from Tempe Hydrolysates using Long Treatment of Fermentation and Proteolytic Enzyme Proportion

Abstract

Tempeh is a native Nusantara food that is often found in traditional Indonesian markets. Over fermentation, due to unsold, they are called over fermented tempeh resulted in non-optimum utilization. Alternative utilizations that can be used is as a seasoning. The making of seasoning can be done by the hydrolysis technique using the protease enzyme of biduri and papain. This study aimed to determine the effect of fermentation time and the proportion of proteolytic enzyme on the physicochemical and organoleptic properties of seasoning from tempeh hydrolysates. The experimental design used was a factorial pattern CRD with two factors. Factor I is tempeh fermentation time (18 hours and 72 hours), while factor II is the enzyme proportion of biduri and papain (0%: 100%; 25%: 75%; 50%: 50%; 75%: 25%; and 100 %: 0%). The best treatment is 72 hours fermentation duration and the enzyme proportion of biduri and papain (50%: 50%) which produces a seasoning powder with the following characteristics: the degree of hydrolysis 82.32%; dissolved protein 58.85%; moisture 7.89%; water solubility index 0.09 gr/ml; oil absorption 0.78 ml/gr, yield 9.32%, organoleptic to taste 3.93 (savory), aroma 3.40 (somewhat pleasant), and color 1.13 (very not white), and glutamic acid content 59, 93 mg/100 gr.

Utilization of Partially Purified Papain Enzyme in Mallika Black Soybean Tempeh Hydrolysate as Umami Seasoning

“…The degree of hydrolysis indicates the percentage of released peptides during the hydrolysis reaction (Putri et al, 2020). Fermentation time and concentration of partially purified papain enzyme added showed significant differences (< 0.05), as displayed in Table 1 degree of hydrolysis increased until it reached its peak on the fourth day of fermentation, and 1% addition of partially purified papain enzyme by 43.64±1.99%.…”

“…Some amino acids bound with water were assumed of lysine and arginine, which had positive charges on side groups; otherwise, glutamic acid and aspartic acid had negative charges. Another amino acid that could bind water was amino acids with hydroxyl groups such as serine and threonine, as well as amide groups of asparagine and glutamine (Putri et al, 2020).…”

“…On the third day of fermentation, the protein content increased, indicating that the enzymatic degradation process remained taking place at high enzyme concentrations. The increased dissolved protein content in hydrolysates occurred because of the breakdown of protein into peptone, small chain peptides, and several soluble amino acids detected by the Lowry reagent (Putri et al, 2020). The presence of peptides was caused by the papain enzyme's mechanism in breaking the peptide bonds.…”