Agriculture Reference
In-Depth Information
B
ETA
-G
ALACTOSIDASE
A basic 55-kDa glycosylated beta-galactosidase (PsBGAL), with N-
terminal sequence resemblance to its counterpart from
Arabidopsis thaliana
,
has been purified from pea seeds by over 900-fold. The enzyme can hydrolyze
pea seed xyloglucan, and may play a role in changing the cell wall
composition in seedling growth and development. (Dwevedi and Kayastha,
2009).
I
NSOLUBLE
A
CID
I
NVERTASE
Invertase catalyzes sucrose hydrolysis into D-glucose and D-fructose. The
69-kDa insoluble acid invertase from pea displays an isoelectric point of about
pH 8.0, a pH optimum of 4.0 and a temperature optimum of 45 °C, a K(m) of
4.41 mM and a V(max) of 8.41 U (mg protein)(-1) min(-1).The enzyme has
been purified by ammonium sulfate precipitation, ion exchange
chromatography, absorption chromatography, reactive green-19 affinity
chromatography, and gel filtration. The activity of the enzyme is unaltered by
Tris-HCl and mercury chloride but inhibited by 6.2 mM copper sulfate. Its pH
optimum and temperature optimum are respectively lower and higher than
other invertases(Kim et al., 2011).
G
ERMIN
-L
IKE
P
ROTEIN WITH
S
UPEROXIDE
D
ISMUTASE
A
CTIVITY
PsGER1 is a germin-like nodule-associated pea protein with superoxide
dismutase activity resistant to hydrogen peroxide, detergents, and high
temperatures. PsGER1 transcript is found in expanding cells near the
meristematic zone and in the epidermis. It exhibits striking sequence
homology to the N-terminal sequence of a putative plant rhicadhesin (a
bacterial attachment protein) receptor,. However, its location in nodules
indicates functions other than a rhicadhesin receptor needed for the initial
stage of bacterial attachment to root hairs (Gucciardo et al., 2007).
