The consumption of low-calorie artificial sweeteners by patients affected by
diseases linked to sugar consumption may be associated with diverse side effects.
Hence, sweet proteins derived majorly from under-utilized plants have been
proposed as good replacements. The ability of sweet proteins to release
Angiostensin-Converting Enzyme (ACE)-inhibitory peptides was investigated. ACE
mediates arterial vasoconstriction and elevation of its activity is an important
pathogenic mechanism of hypertension. The protein sequences of six sweet
proteins, Thaumatin from Thaumatococcus danielli (NCBI accession number,
gi|209473), Brazzein from Pentadiplandra brazzeana (NCBI accession number,
gi|218218145), Monellin from Dioscoreophyllum cumminsii (NCBI accession
number, gi|381144434), Madinlin from Capparis masaikai (NCBI accession
number, gi|1817546), Curculin from Curculigo latifolia (NCBI accession number,
gi|11225520) and Miraculin from Richadella dulcifica (NCBI accession number,
gi|253735645) were selected for sequence alignment using Basic Local Alignment
Search Tool (BLAST) analysis and biological activity search using BIOPEP. Although
BLAST analysis gave no homologous similarity among the proteins, BIOPEP analysis
showed that they demonstrated either di- or tri-peptide with a total of 51, 14, 40,
28, 30 and 59 potential ACE inhibitory peptides from Thaumatin, Brazzein,
Monellin, Madinlin, Curculin and Miraculin respectively. The combined digestion
with pepsin, trypsin and chymotrypsin A, a simulation of human gastrointestinal
digestion released 8, 2, 9, 2, 5 and 11 ACE inhibitory peptides from Thaumatin,
Brazzein, Monellin, Madinlin, Curculin and Miraculin respectively. These results
add value to these proteins by demonstrating their innate nutraceutical potential in
their ability to reduce hypertension. Table of Content