The anti hypertensive nutraceuticals of Vigna sp bean protein hydrolized by alcalase and flavourzyme

  • Tejasari Department of Agriculture Result Technology, Faculty of Agriculture Technology, University of Jember, Jember-68121, Indonesia
  • Sih Yuwanti Department of Agriculture Result Technology, Faculty of Agriculture Technology, University of Jember, Jember-68121, Indonesia
  • Mohammad Bazar Ahmadi Department of Agriculture Result Technology, Faculty of Agriculture Technology, University of Jember, Jember-68121, Indonesia
  • Yuna Luki Afsari Department of Agriculture Result Technology, Faculty of Agriculture Technology, University of Jember, Jember-68121, Indonesia
Keywords: ACE-I inhibitory ability, alcalase and flavourzyme protease, anti hypertensive  nutraceuticals, solubility of Vigna sp bean protein hydrolysates, Vigna sp bean protein hydrolysates

Abstract

Peptide with hydrophobic amino acids at the end of its chain had been studied in various countries for their inhibitory activity against angiotensin-I converting enzyme (ACE-1) transformation into ACE-2 and therefore prevention of vasoconstriction of blood vessels and high blood pressure (hypertension). The active peptides may come from alcalase and flavourzyme exogenous hydrolysis of bean protein. This study aimed to measure ACE-1 inhibitory ability of protein hydrolysates ofmung bean (Vigna radiata(L) R. Wilzeck) and cowpea (V. unguiculata(L) Walphthat grew in Indonesia, and its solubility for its application purposes. The bean protein content (22.9 -23.6 %) was extracted using isoelectric precipitation method of each at a range pH 4-4.6, centrifuged at 2000-4000 x g for 20 minutes.  The obtainedbean protein extracts were hydrolyzed at pH 8 for alcalase and pH 7 for flavourzyme, at constant stirring of each ranged for 90-120 minutes at 50-55 oC  and inactivated  at 80-85 oC. ACE-1 inhibitory activity was evaluated using spectrophotometry method (228 nm). The amount of hippuric acid (HA) formed by the hydrolysis of Hippuryl-His-Leu(HHL) was calculated to represent the ACE-1 inhibitory activity. Ultra chromatography evaluation in the protein hydrolysates showed higher content of hydrophobic amino acids in mung bean protein (382 mg/g protein) compared to those in cowpea protein (329 mg/g protein). Higher ACE-I inhibitory activities were observed in protein hydrolysates of the two vigna beans that were hydrolyzed by alcalase enzymes rather than by flavourzyme.The Vigna spp bean protein that went into hydrolysis by alcalase, produced small molecular weight peptides (3.9-4.63 kDa), with high ACE-I inhibition ability (80-93 %), Therefore, this protein hydrolysate might be suggested as antihypertensive nutraceuticals. Highest solubility of protein hydrolysates resulted from alcalase hydrolysis of mung bean and cowpea protein were observed at pH 8, while those resulted from flavorzyme hydrolysis were at pH 7, respectively. 

Published
2020-08-31
How to Cite
Tejasari, Yuwanti, S., Ahmadi, M. B., & Afsari, Y. L. (2020). The anti hypertensive nutraceuticals of Vigna sp bean protein hydrolized by alcalase and flavourzyme. Journal of Functional Food and Nutraceutical, 2(1). https://doi.org/10.33555/jffn.v2i1.40
Section
Articles