Biomedical Engineering Reference
In-Depth Information
Chapter 13
A
CACIA
C
AVEN
(M
OL
.) M
OLINA
P
OLLEN
P
ROTEASES
. A
PPLICATION TO THE
P
EPTIDE
S
YNTHESIS AND TO
L
AUNDRY
D
ETERGENTS
Cristina Barcia
1
, Evelina Quiroga
1,3,a
, Carlos Ardanaz
2
,
Gustavo Quiroga
1
and Sonia Barberis
1,3,b
1
Laboratorio de Bromatología
2
Área de Química Orgánica. Facultad de Química, Bioquímica y Farmacia. Universidad
Nacional de San Luis. Chacabuco y Pedernera (5700) San Luis, Argentina
3
Instituto de Física Aplicada (INFAP). Universidad Nacional de San Luis, Argentina
Abstract
It is known that the proteases have applications in several industrial processes such us leather
processing, laundry detergents, producing of protein hydrolysates and food processing, as well
as in the peptide synthesis in non conventional media. The application of proteases as catalyst
of short oligopeptides in aqueous-organic media, have received a great deal attention as a
viable alternative to chemical approach because of their remarkable characteristics. On the
other hand, alkaline proteases have also been used to improve the cleaning efficiency of
detergents. Detergent enzymes account for about 30% of the total worldwide enzyme
production and represent one of the largest and most successful applications of modern
industrial biotechnology. The aim of this work was to study the performance of proteolytic
enzymes of
Acacia caven
(Mol.) Molina pollen for its potential application as an additive in
various laundry detergents formulations and as catalyst of the peptide synthesis in aqueous-
organic media. Pollen grains (35 mg/ml) were suspended in 0.1M Tris-HCl buffer pH 7.4 and
slowly shaken for 2 h at 25° C. Then, the slurry was centrifugated for 30 min at 8000 rpm and
the supernatant (crude enzyme extract, CE) was tested in protein content (Bradford's method)
and proteolytic activity (using BAPNA and Z-Ala-pNO as substrates). A partial
characterization of
Acacia caven
CE was carried out: enzyme extract displayed maximum
proteolytic activity at pH 8 and 35-40º C; it showed remarkable thermal stability after 1.5 h at
25-40º C but it decreased as long as temperature increased to 60º C. On the other hand, the
enzyme extract was incubated with different surfactants and commercial laundry detergents at
a
E-mail address: equiroga@unsl.edu.ar. (Corresponding author: Evelina Quiroga)
b
E-mail address: sbarberi@unsl.edu.ar (Corresponding author: Sonia Barberis).
