Galactomannan reserves in the endosperm of intact fenugreek (Trigonella foe
num-graecum) seeds were mobilized in part by endo-beta-D-mannanase (mannan
endo-1,4-beta mannosidase, E beta M, EC 3.2.1.78) activity. The hydrolytic
products, mannose and galactose, applied to isolated endosperms at physiolo
gically relevant concentrations enhanced E beta M activity; but at higher c
oncentrations, E beta M activity and its secretion were inhibited. Increase
s in glucose, fructose, and sucrose in the embryo reflected the mobilizatio
n of the galactosyl-sucrose sugars therein and, presumably, the uptake of t
he hydrolytic products of galactomannan breakdown from the endosperm. Concu
rrent with the accumulation of both axial and cotyledonary starch, with tim
e and with the incubation of isolated seedlings in sugar solutions, there w
ere increases in the steady state amounts of transcripts of both the large
and small subunits of adenosine diphosphate glucose pyrophosphorylase (gluc
ose-1 -phosphate adenylyl-transferase, EC 2.7.7.27), the key regulatory enz
yme of starch synthesis. The corresponding sugar, adenosine diphosphoglucos
e, accumulated only within the cotyledons after starch began to decrease. A
ctivity of the starch degradative enzyme Fenugreek (TrigoMelln foenum-gmecu
m L.) seedlings present an interesting opportunity to study the regulation
of carbohydrate mobilization following germination because three different
types of carbohydrates (galactomannans, soluble sugars including the,oalact
osyl-sucrose sugars, and starch) are utilized dur ing their establishment [
15-18]. The major source of stored carbohydrate reserves in the dry fenugre
ek seed is the galactomannan contained within the endosperm cell walls [16]
. These are mobilized during early seedling growth following the production
and secretion of hydrolytic enzymes (agalactosidase (EC 3,2,1.22), P-manno
sidase (EC 3.2.1.25), and mannan endo-1,4-P mannosidase (EC beta-amylase (E
C 3.2.1.2) increased in the cotyledon as starch started to decline, althoug
h low amounts of alpha-amylase (EC 3.2.1.1) were constitutively present. (C
) Elsevier, Paris.