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Investigating carotenoid loss after drying and storage of

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35<br />

1. Literature review<br />

Enzymatic cleavage <strong>of</strong> <strong>carotenoid</strong>s in plant is catalysed by a family <strong>of</strong> non-heme<br />

<strong>carotenoid</strong> cleavage dioxygenases (CDDs) that can cleave regiospecifically the 9,10 or<br />

11,12 double bonds <strong>of</strong> <strong>carotenoid</strong>s leading to apo<strong>carotenoid</strong> products (Auldridge et al.<br />

2006; Huang et al. 2009). Alternatively enzymatic cleavage leading to apo<strong>carotenoid</strong><br />

products can be operated unspecifically by co-oxidation (Bosser <strong>and</strong> Belin 1994). Co-<br />

oxidation <strong>of</strong> <strong>carotenoid</strong>s <strong>and</strong> another substrate, for instance fatty acids, such as linoleic<br />

acid, using lipoxygenase <strong>and</strong> xanthine oxidase has been extensively studied by Bosser et<br />

al. (1995) <strong>and</strong> Waché (2002; 2003; 2006). It has been reported that <strong>carotenoid</strong>s are<br />

oxidised by free radical species generated from another substrate by enzymatic reactions<br />

(Waché et al. 2002; Zorn et al. 2003).<br />

Co-oxidation <strong>of</strong> β-carotene by lipoxygenase from potato (Solanum tuberosum) has been<br />

reported (Aziz et al. 1999). Presence <strong>of</strong> lipoxygenase has also been reported in cassava<br />

(Isamah 2004), but it has not yet been identified in sweet potato. On the other h<strong>and</strong>,<br />

sweet potato is reported as an excellent source <strong>of</strong> peroxidase activity, which is mostly<br />

situated in the peel (Castillo-Leon et al. 2002). Peroxidases can also generate free radical<br />

species (Yamazaki et al. 1985). Cleavage <strong>of</strong> β-carotene by peroxidase secreted by the<br />

fungus Lepista irina was reported by Zorn et al. (2003). Cleavage products were the<br />

same as with CDDs cleavage or co-oxidation by lipoxygenases or xanthin oxidases<br />

(Zorn et al. 2003). However in studies on higher plants, catabolism <strong>of</strong> <strong>carotenoid</strong>s by<br />

peroxidase was reported to be dependent on the addition <strong>of</strong> a phenolic substrate (2,4<br />

dichlorophenol) (Matilde <strong>and</strong> Martinoia 1982; Kennedy et al. 2002; G<strong>and</strong>ul-Rojas et al.<br />

2004) <strong>and</strong> was enhanced by the further addition <strong>of</strong> hydrogen peroxide (Matilde <strong>and</strong><br />

Martinoia 1982). In order to determine the causes (enzymatic or non-enzymatic) <strong>of</strong><br />

<strong>carotenoid</strong> degradation one should take into account the presence <strong>of</strong> these substrates.<br />

1.3.5 Products <strong>of</strong> degradation<br />

"-carotene is degraded in a chain radical propagation reaction. The products <strong>of</strong> oxidation<br />

<strong>of</strong> "-carotene are diverse <strong>and</strong> include: high molecular weight products, such as, various<br />

apo-β-carotenal (8’; 10’; 12’; 14’; 15’), that further degrade; <strong>and</strong> short chain products,<br />

such as, fragrant compounds called norisoprenoids (Siems et al. 2005)

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