PRODUCTION OF ANTIOXIDANT HYDROLYSATES FROM

QUINOA PROTEINS USING A BACILLUS SPP. ALKALINE

SERINE PROTEASE
Elena Peñas1, Luz Paucar-Menacho2, Juana Frias1 , Cristina Martinez-Villaluenga1
1Instituto de Ciencia y Tecnología de Alimentos y Nutrición (ICTAN-CSIC), Madrid 28006, España
2Departamento de Ingeniería Agroindustrial, Universidad Nacional del Santa, Nuevo Chimbote, Ancash, Perú

INTRODUCTION
Quinoa has been recognized by FAO as one of the crops destined to provide food security in the XXI century mainly because its high protein content
and quality (1). This pseudocereal is of nutritional interest mainly due to the high concentrations of proteins, minerals, vitamins and health-
promoting bioactive compounds. Quinoa proteins are rich in amino acids like lysine, which is deficient in cereals, and it does not contain gluten (2).
Besides nutritional features, there is increasing scientific outcomes which demonstrate that quinoa proteins are sources of bioactive peptides. The
interest for antioxidant peptides has increased thanks to the abundant evidences of the in vivo prevention of oxidative stress, which are mainly
associated to degenerative aging diseases (3). Literature has reported the application of antioxidant peptides from animal proteins, however, quinoa
enzymatic proteolysis has been less explored for that purpose so far.

OBJECTIVE
The aim of this study was to produce antioxidant hydrolysates from quinoa (Chenopodium quinoa var. Pasankalla) protein concentrates using
Savinase® 16 L, an alkaline serine protease from Bacillus spp.

MATERIAL AND METHODS

 Protein pattern (SDS-PAGE)
Suspension in water (2%, w/v)
 Degree of hydrolysis (DH)
Savinase®16 L (0.1 U/mg protein)  Peptide content (DC Protein Assay Kit): <3 kDa (LMW) and <10 kDa (MMW)
Quinoa Protein at 37 ºC for 0-180 min  Antioxidant activity (ORAC)
(var. Pasankalla) concentrate (82%)

RESULTS
Peptide content Degree of hydrolysis
ORAC
mmol trolox/mg ptotein

10 30 800
free amino groups

8
(mmol/L)

20 600
6 LMW
mg/g

4 MMW
10 400
2
0 0 200
0 50 100 150 200 0 50 100 150 200
0 50 100 150 200
Time (min) Time (min) Time (min)

Protein pattern MW (kDa)  Savinase showed a high proteolytic efficiency degrading completely the main proteins of quinoa
(7S and 11S globulins) and releasing peptides < 10 kDa.
260
160  The highest degree of hydrolysis was reached after 150 min of Savinase treatment.
110
80  The highest content of MMW and LMW peptides was reached after 120 and 180 min,
60 respectively.
50
 Quinoa protein hydrolysates were characterized mainly by LMW peptides accounting for more
40
than 75% of the total protein content.
30
 Antioxidant activity increased gradually with hydrolysis time. Maximum ORAC values were
20
found at 180 min (775 mmol Trolox equivalents/mg protein).
15
10

3.5 CONCLUSION
Hydrolysates from quinoa seeds have a promising potential to be used as functional ingredients or
O 30 60 90 120 150 180 Control MK
nutraceuticals to prevent from in vivo oxidative cell damage of free radicals or to be incorporated as
Time (min)
natural additives to enhance food preservation.

REFERENCES
(1) FAO & CIRAD, 2015. State of the Art Report of Quinoa in the World in 2013. ACKNOWLEDGEMENTS
In D. Bazile & D. B. C. Nieto (Eds.). Rome. This research was funded by the Ministry of Economy and Competitiveness (Spain) and FEDER
(2) Ferreira et al. 2015. Food Control, 48: 91-95. programme through the project AGL2013-43247-R. E. Peñas thanks to Ramón y Cajal Programme
(3) Samaranayaka, et al. 2011. J. Funct. Foods, 3: 229-254. and L.M. Paucar-Menacho to Consejo Nacional de Ciencia y Tecnologia (Peru).