Physicochemical and Flavor Characteristics of Flavoring Agent from Mungbean Protein Hydrolyzed by Bromelain

Abstract

Enzymatic bromelain mungbean meal protein hydrolysate (eb-MPH) was produced from mungbean meal protein isolate (MPI). Enzymatic bromelain, with a known protease activity of 98,652 (unit/g), was used at concentrations of 0, 2, 6, 10, 14 and 18% (w/w) and with hydrolysis times of 0.5, 3, 6, 12, and 24 h. The pH and temperature were controlled at 6.0 and 50 °C, respectively. It was found that the best treatment combination for eb-MPH production by response surface methodology (RSM) was 18% bromelain and a hydrolysis time of 3 h, resulting in the greatest degree of hydrolysis (% DH) and percent yield, with values of 61.04 and 45.63%, respectively. Results also showed that the phenylalanine, tyrosine and leucine contents of the optimally produced eb-MPH were 20.88, 14.50 and 10.93%, respectively. Twelve volatile compounds were identified using gas chromatography mass spectrometry in eb-MPH; benzaldehyde, 2-pentylfuran and furfural were the predominant odorants.

Assessment of antioxidant properties of membrane ultrafiltration peptides from mungbean meal protein hydrolysates

“…Crude-MMPH contained highly hydrophobic amino acids (HAA) due to the hydrolysis using bromelain which is an endoprotease which cleaves at hydrophobic position inside the protein chain. Bromelain has specific cleavage preference at Arg, Lys and Phe sites, resulting in the rich HAA observed in this study (Adler-Nissen, 1986;Sonklin, Laohakunjit & Kerdchoechuen, 2011). F4 had the highest proportion of aromatic and hydrophobic amino acids when compared to other peptide fractions and combined with F4 contained low molecular weight peptide less than 1 kDa.…”

“…The peptides derived from these enzymes, possessed antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities (Lapsongphon & Yongsawatdigul, 2013;Li et al, 2006). Previous studies have shown that mungbean hydrolysed using bromelain could generate flavour peptides that have umami flavour characteristics and also antioxidant properties (Sonklin, Laohakunjit & Kerdchoechuen, 2011;Sonklin et al, 2018). While the antioxidant properties from mungbean protein hydrolysate have been reported, the capability of the peptide fractions to retain these activities lacks of information.…”

Bromelain: an overview of industrial application and purification strategies

“…For example, the hydrolysis of mungbean protein by bromelain has released 16 free amino acids which give a meaty flavor characteristic such as bouillon, sweet smell, green, and fatty (Sonklin et al 2011). Besides, after bromelain hydrolysis, several amino acids such arginine, lysine, and leucine were found from the protein byproduct hydrolysis of Gracilaria fisheri (red seaweeds) which characterize seafood flavoring (Laohakunjit et al 2014).…”

A novel multi-biofunctional protein from brown rice hydrolysed by endo/endo-exoproteases

“…8 Apart from their functionalities, the 5-10 kDa fractions of enzymatic protein hydrolysates from different plant protein sources possess unique taste properties, including sweet, salty, bitter, and umami tastes. 2,5,9,11,12 In addition to these cereals, brown rice protein is a good plant protein source because rice proteins are a gluten-free and less allergenic food grain. 9 Most peptides with a high molar ratio of L-glutamic acid peptides and a hydrophilic C-terminal residue have also been reported to elicit an intense umami taste.…”

“…Although the protein content of rice is not particularly high (7-9 g per 100 g), rice protein contains the complete essential amino acids, particularly lysine, which is a limited amino acid in other cereals 13 and has been reported to be an antioxidative amino acid. 1,11 Nevertheless, endo-exoproteases, such as Flavourzyme® and PROTEASE FP51®, were applied to reduce the undesirable bitterness of protein hydrolysate. However, the application of rice protein as a nutritious and functional food is still limited because it consists mainly of alkali-soluble glutelin (∼80%), which exhibits poor solubility and low digestibility at acidic and neutral pH.…”