Agriculture Reference
In-Depth Information
Ca2+/calmodulin-dependent protein kinase, enzyme catalyzing
conjugation of indole-3-acetic acid to aspartate, pea albumin 1F (PA1F),
pea albumin 1, subunit b, vicilin, lectins, mitochondrial type II
peroxiredoxin, channel-forming protein in chloroplasts, outer envelope
membrane protein 16 of pea chloroplasts, cell wall fibronectin-like
adhesion protein, arabinogalactan-protein-extensin glycoproteins, ferritin,
and dehydrin.
Keywords:
pea,
Pisum sativum
, proteins, enzymes
I
NTRODUCTION
Peas are rich in proteins and dietary fiber and contribute considerably to
the total dietary protein requirements. Peas are abundant in complex
carbohydrates giving rise to food with a low glycemic index. Peas are
hypolipidemic. Fiber in peas contains more amylose than amylopectin and is
antihyperglycemic. Peas can be used in processed foods such as bakery
products, bread, snack foods, soups, and tortillas. Because of their
nutritiousness, it has been suggested that peas be included in snack foods, baby
food, and sports food (Asif et al., 2013).
The purpose of this article is to review the pea enzymes and proteins
reported in the literature.
A
LPHA
-G
ALACTOSIDASES
Two cDNAs encoding alpha-galactosidases from maturing and
germinating pea seeds, including a member of the acidic alpha-galactosidase
of the family 27 glycosyl hydrolase cluster and a member of the family of
alkaline alpha-galactosidases, which display pronounced homology to seed
imbibition proteins, have been isolated. Transcripts encoding the acidic alpha-
galactosidase, found in protein storage vacuoles, are present in dry seeds and
expressed during seed maturation and exhibit little variations in seed
germination. Transcripts encoding the alkaline alpha-galactosidase are
expressed after radicle protrusion (Blöch et al., 2008).
