title: Enzyme technology for precision functional food ingredient processes.
abstract: A number of naturally occurring dietary substances may exert physiological benefits. The production of enhanced levels or particularly tailored versions of such candidate functional compounds can be targeted by enzymatic catalysis. The recent literature contains examples of enhancing bioavailability of iron via enzyme-catalyzed degradation of phytate in wheat bran, increasing diacyl-glycerol and conjugated linoleic acid levels by lipase action, enhancing the absorption of the citrus flavonoid hesperetin via rhamnosidase treatment, and obtaining solubilized dietary fiber via enzymatic modification of potato starch processing residues. Such targeted enzyme-catalyzed reactions provide new invention opportunities for designing functional foods with significant health benefits. The provision of well-defined naturally structured compounds can, moreover, assist in obtaining the much-needed improved understanding of the physiological benefits of complex natural substances.
authors.affiliation: BioProcess Engineering Center, Department of Chemical and Biochemical Engineering, Technical University of Denmark, Lyngby, Denmark. am@kt.dtu.dk
authors.forename: Anne S
authors.initials: AS
authors.lastname: Meyer
mesh_terms: D010832:6-Phytase / Q000235:genetics / Q000378:metabolism; D000818:Animals; D001709:Biotechnology / Q000379:methods*; D004043:Dietary Fiber / Q000378:metabolism; D004798:Enzymes / Q000235:genetics / Q000378:metabolism*; D005524:Food Technology / Q000379:methods* / Q000592:standards; D055951:Functional Food; D006026:Glycoside Hydrolases / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008049:Lipase / Q000235:genetics / Q000378:metabolism; D010833:Phytic Acid / Q000378:metabolism; D011096:Polygalacturonase / Q000235:genetics / Q000378:metabolism
chemical_list: D004043:Dietary Fiber; D004798:Enzymes; D010833:Phytic Acid; D008049:Lipase; D010832:6-Phytase; D006026:Glycoside Hydrolases; C023307:hesperidinase; D011096:Polygalacturonase