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enzymatic protein hydrolysates and ultrafiltered peptide fractions from cowpea vigna unguiculata l bean with in vitro antidiabetic potential
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نویسنده
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castañeda-pérez eduardo ,jiménez-morales karina ,quintal-novelo carlos ,moo-puc rosa ,chel-guerrero luis ,betancur-ancona david
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منبع
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journal of the iranian chemical society - 2019 - دوره : 16 - شماره : 8 - صفحه:1773 -1781
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چکیده
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Diabetes mellitus (dm) is a disease that affects an increasing number of people worldwide consisting on a rise in blood sugars levels. diabetes mellitus type 2 (dmt2) is the most common and accounts for 95% of cases. in this work, the antidiabetic potential of cowpea (vigna unguiculata l.) protein hydrolysates (ph) and ultrafiltered peptide fractions (ufpf) by means of the in vitro inhibition of the α-amylase, α-glucosidase, and dipeptidyl peptidase iv (dpp-iv) enzymes were analyzed. their cytotoxicity was also assessed in healthy vero cells lines to assess their safety as possible ingredients in food. the cowpea proteins were hydrolyzed with alcalase®-flavourzyme® sequential system. their highest inhibitory activities were: f > 10 kda to inhibit α-amylase, f > 10 kda and ph to inhibit α-glucosidase, and ph to inhibit dpp-iv. their ic50 values were 31.58, 0.633, 1.81, and 2.06 mg protein per ml, respectively. in a second experiment, phs and ufpfs were hydrolyzed with a pepsin–pancreatin sequential system and showed the following inhibitory activities: f1–3 kda and f < 1 kda to inhibit α-amylase, and f < 1 kda to inhibit α-glucosidase. their ic50 values were 65.79, 40.17, and 189.04 mg protein per ml, respectively. the degree of hydrolysis was extensive for all the phs and the highest was obtained using the alcalase®-flavourzyme® sequential enzyme system. the phs and ufpfs with the highest inhibitory activity of the α-amylase, α-glucosidase, and dipeptidyl dpp-iv enzymes did not show in vitro cytotoxicity activity in vero cells. therefore, they are potential ingredients to produce functional food for patients with dmt2.
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کلیدواژه
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antidiabetic potential ,protein hydrolysates ,peptide fractions ,cowpea ,vigna unguiculata l
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آدرس
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universidad autónoma de yucatán, méxico, universidad autónoma de yucatán, méxico, instituto mexicano del seguro social, unidad médica de alta especialidad hospital de especialidades-1 mérida, méxico, instituto mexicano del seguro social, unidad médica de alta especialidad hospital de especialidades-1 mérida, méxico, universidad autónoma de yucatán, méxico, universidad autónoma de yucatán, méxico
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Authors
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