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Volume 8
Journal of Biotechnology & Biomaterials
ISSN: 2155-952X
Biotech Congress 2018 & Enzymology 2018
March 05-07, 2018
JOINT EVENT
20
th
Global Congress on
Biotechnology
3
rd
International Conference on
Enzymology and Molecular Biology
&
March 05-07, 2018 London, UK
Enzymatic production of bioactive peptides from raps flour
Ferrero Romina Lis
Pontificia Universidad Católica de Valparaíso, Chile
T
he biologically active peptides may exert systemic effects, such as antihypertensive, antioxidant, antiproliferative, among
others. The defatted flour of raps, a byproduct of rape oil, has between 30-40% of proteins, being an interesting source for
the production of bioactive peptides. Given this, our goal is to obtain peptides with different degrees of hydrolysis, in order
to study their ability to inhibit the proliferation of MCF-7 cells (breast cancer) as part of their biological properties. Protein
from rape flour was recovered by alkaline solubilization and isoelectric precipitation. Afterwards, the peptides were obtained
by enzymatic hydrolysis with Alcalase® 2.4 L (50 °C), analyzing two processes, one without pH adjustment (starting at pH 10)
and another controlling the pH at 8 (optimum pH of the enzyme), by means of a pH-stat, at enzyme/substrate ratios of 3 and
5%, for a time of 24 h. The degree of hydrolysis was measured by the method of orthophthaldehyde (OPA) and antiproliferative
activity by the resazurin method. The hydrolysis kinetics obtained, showed that by controlling the pH at 8 throughout the
reaction, the enzymatic rate is higher and thus the degree of hydrolysis, reaches up to 22% at 20 hours when using 3% of
enzyme. With regards to antiproliferative activity, it is possible to determine an inhibition of MCF-7 cell proliferation of up to
80% when a 10 mg/L peptic extract is used, demonstrating the effectiveness of the enzymatic treatment with Alcalase® 2.4 L to
obtain peptides with potential anticancer activity.
romi.ferrero@hotmail.comJ Biotechnol Biomater 2018, Volume 8
DOI: 10.4172/2155-952X-C2-092