S. Berghall et al., THE ROLE OF SUGAR-BEET INVERTASE AND RELATED ENZYMES DURING GROWTH, STORAGE AND PROCESSING, Zuckerindustrie, 122(7), 1997, pp. 520-530
In a collaborative project between British Sugar pie and Sucros Ltd, f
our sucrose inverting enzyme activities were identified in sugar beet:
soluble acid invertase, insoluble acid invertase, soluble alkaline in
vertase and soluble sucrose synthetase. The activities of these enzyme
s were measured in the growing crop, during beer storage and through t
he extraction process. Crop sample results confirmed many of the previ
ous understandings on the phasing of plant growth and sucrose accumula
tion. It is likely that the enzymes active in sugar beet before harves
t are necessary in their entirety for healthy plant development. Durin
g clamping and storage, a relationship between beet invertase and sucr
ose synthetase activities? and invert sugar content was observed. Two
distinct physiological pathways influencing these activities are propo
sed. Clamping and storage trials were performed both in U.K, and Finla
nd under very different climatological conditions. Typical late autumn
and early winter freezing and thawing in Finland caused significant i
nvertase activity increase in beet starting to deteriorate. Microbial
invertases analysed showed significantly higher thermostability compar
ed to beet invertases. Results from healthy beet process sampling indi
cated that only a small fraction of the difference between sugar beet
and raw juice invert sugar concentration was due to sugar beet derived
invertase enzymes. While processing frozen and thawed beet material,
the invert sugar difference was higher, but still only partially expla
ined by elevated invertase enzyme activities in the beet material. The
results emphasized the importance of rapid temperature increase in ex
traction. It is possible to estimate the considerable financial impact
of invert sugar formation during clamping and processing. This report
provides information useful in the reduction of this cost.