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Chemical and Functional Properties of Food Saccharides

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© 2004 by CRC Press LLC<br />

compounds such as para-nitrophenyl galactosyl chromogens, various chiral sugar<br />

derivatives, <strong>and</strong> disaccharides such as galactosyl- xylose. 25<br />

Generally, the molecules <strong>of</strong> β-GOS can be presented as:<br />

Gal X (Gal) n Y Glc<br />

where n is the number <strong>of</strong> β-1,4-linked galactose residues; x = β-1,6 > β-1,4, β-1,3;<br />

<strong>and</strong> y = β-1,2, β-1,6 > β-1,4. This formula indicates that apart from the dominating<br />

β-1,4 glycosidic bond, β-galactosidases synthesize some β-1,3 <strong>and</strong> β-1,6 linkages<br />

too.<br />

Apart from galactooligosaccharides, lactulose, tagatose, <strong>and</strong> lactobionic acid can<br />

also be obtained from lactose, using relevant oxidoreductases (see Section 10.2.6).<br />

Because lactose is an attractive starting material, the list <strong>of</strong> its derivatives continues<br />

to grow. For example, hexyl glycosides have been prepared by lactose hydrolysis<br />

with β-galactosidase, followed by a treatment with thermostable β-glycosidases from<br />

hyperthermophiles. 26 It should be emphasized that their hydrolysis with α-galactosidase<br />

preparations enhances digestibility <strong>of</strong> certain plant foods. 27 α-Galactosidases<br />

are also applicable for synthesis <strong>of</strong> the so-called globo-oligosaccharides, having<br />

terminal α-D-galactose-1,4-α-D-galactose sequences <strong>and</strong> involved in interactions<br />

with pathogens <strong>and</strong> viruses.<br />

10.4 POLYSACCHARIDES<br />

10.4.1 STARCH<br />

The application <strong>of</strong> enzymes in industrial starch processing dates back to the 1970s.<br />

Currently, amylolytic enzymes constitute approximately 30% <strong>of</strong> total market <strong>of</strong><br />

biocatalysts. Starch-converting enzymes, listed in Table 10.4, comprise endo- <strong>and</strong><br />

exoamylases, debranching enzymes, <strong>and</strong> transferases. 11 Their majority (except glucoamylase<br />

<strong>and</strong> β-amylase) belong to the α-amylase family, comprising numerous<br />

hydrolases <strong>and</strong> transferases, though some are active against substrates other than<br />

starch or dextrins. Enzymes <strong>of</strong> Family 13 <strong>of</strong> GHs, with a retaining mechanism <strong>of</strong><br />

attack, dominate the α-amylase family, but some catalytic proteins assigned to the<br />

Family 70 (dextransucrase <strong>and</strong> alternansucrase) <strong>and</strong> Family 77 (4-α-glucanotransferase)<br />

GHs also share the structure <strong>of</strong> the catalytic domain [in the form <strong>of</strong> (β/α) 8<br />

barrel] <strong>and</strong> mechanism <strong>of</strong> the action with α-amylase.<br />

Apart from amylolytic enzymes, some other enzymatic activities are also found<br />

to be necessary for a satisfactory degree <strong>of</strong> large-scale starch conversion. For<br />

instance, enzymatic starch processing has to face some problems related to the<br />

presence <strong>of</strong> amylose–lipid complexes formed either in situ in wheat starch granules<br />

or generated on gelatinization <strong>of</strong> containing lipids starch slurries. Lipases, mainly<br />

lysophospholipases, are applied together with amylolytic enzymes to improve the<br />

yield <strong>of</strong> processing.

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