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ANTI-NUTRITIONAL CONSTITUENT OF COLOCASIA ESCULENTA ...

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calcium metalloenzymes, are completely unable to function. MacGregor et al., (2001)<br />

commented that these amylases are crucial to the carbohydrate metabolism of many<br />

autotrophic and heterotrophic organisms.<br />

a-Amylase catalyzes the break down of 0.-(1,4) glycosidic linkages found in starch<br />

components and other related carbohydrates (DoleekoVli-MareSova et al., 2005). In<br />

autotrophic organisms, sugars are gradually released from starch which has previously<br />

been stored, thus providing energy for proper growth. Amylases have established many<br />

valuable functions within society, some of which are disease testing, fruit ripening and<br />

malt production (Teotia et al., 2001). a-Amylases also play a major part in breaking<br />

down starch in germinating seeds (Jones and Jacobsen, 1991). Usually, the major<br />

constituent ofman's diet is carbohydrate and the main carbohydrate ingested is starch. a­<br />

Amylases are the most important means heterotrophic organisms use to digest starch<br />

(Silva et at., 2000).<br />

Several compounds found in nature are responsible for inhibiting enzymes, especially the<br />

hydrolases (Kokiladevi, 2005). Current investigations in the field of proteinase and<br />

amylase inhibitors and the growing interest in these phytochemicals in industry and<br />

pharmacy have led researchers to inquire directly into their exact biological function.<br />

Some of these inhibitors are proteins which decrease specific enzyme activities, such as<br />

the inhIbitors ofproteases and amylases (Whitaker and Feeney, 1973).<br />

In 1934, Chrzaszcz and Janicki identified AI in wheat and since then, numerous studies<br />

have recognized the fact that a-amylase inhibitors occur naturally in a wide variety of<br />

plants. Richardson (1991) and Franco et al. (2002) proposed that a-Amylase inhibitors<br />

may simply be classified by their tertiary structure into six different classes, which<br />

researchers identify as lectin-like, knottin-like, cereal-type, Kunitz-like, y-purothionin­<br />

like and thautamin-like. The molecular weight, disulfide bond content, three-dimensional<br />

structure and stability to heat and denaturing agent (Teles et at., 2004) differentiate<br />

among these families. Each family of a-amylase inhIbitors shows particular specificity<br />

features:<br />

120

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