ANTI-NUTRITIONAL CONSTITUENT OF COLOCASIA ESCULENTA ...

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ACKNOWLEDGEMENTS The work presented in this thesis has been carried out at the University of Zululand, KwaDlangezwa, Empangeni, South Africa I would like to thank all the people that contributed to this thesis. • My promoter, Professor Andy Opoku (Department of Biochemistry), for your support and encouragement. Thank you for keeping me focused during the stressful times. • My co-promoters Professor T Djarova (Department ofBiochemistry) and Dr OA Oyedeji (Department ofChemistry). • Professor Djarova, thank you for directing and providing me with invaluable advice. • Bola if it wasn't for you helping me with characterization of saponin I would never have finished - thank you for assisting and encouraging me when my moral was low. • My darling husband Andrew for all your help, especially with feeding the rats! Also your love and endless support, always being positive and putting me and the completion ofthis thesis first. • My daughter, Chante for being so patient with me while I worked such long hours - thank you, you are a little star. • My mom and dad for all the love and support. • All the technical help: • Anita, Brett and Dilip at the University of Kwazulu-Natal for providing your apparatus and expertise and help. • Piet Oosthuizen for providing Amadumbe from Makatini Research farm. • Lina Wallis from Capital Lab for providing me with all the chemicals. 1ll
Page 1 and 2: ANTI-NUTRITIONAL CONSTITUENT OF COL
Page 3: ABSTRACT Colocasia esculenta 1. Sch
Page 7 and 8: ABSTRACT ACKNOWLEDGEMENTS LIST OF A
Page 9 and 10: A.4.2.1 A.4.2.2 A.4.3 A.4.4 CHAPTER
Page 11 and 12: B.5.2 REFERENCES SECTION C EFFECTS
Page 13 and 14: ACAT ALT AI AlA AOAC apoB AST ATP A
Page 16 and 17: Figure BI-3.6 Figure B2-1.1 Figure
Page 18 and 19: TableA3-la TableA3-lb TableA3-lc Ta
Page 20 and 21: CHAPTER 1: GENERAL INTRODUCTION Nut
Page 22: SECTION A PROXIMATE COMPOSITION AND
Page 25 and 26: Plants of the genus Colocasia are e
Page 27 and 28: Colocasta esculenta (L.) Schott is
Page 29 and 30: A.l.3 A.1.3.1 A.1.3.2 acquired an i
Page 31 and 32: • seed development and mobilizati
Page 33 and 34: A protein which inactivates trypsin
Page 35 and 36: A.l.4.3 Hollenbeck et al., 1983; Ca
Page 39: A.I.4.S 1977), (Hagerman and Butler
Page 44 and 45: The ability of phytic acid to compl
Page 47: Cytochrome oxidase, the terminal ox
Page 50 and 51: .- harvest, packaging, storage cond
Page 52: A.2.1 Introduction A.2.2 A.2.2.1 A.
Page 55 and 56:
A.2.3.3 A.2.3.4 U.3.4.1 iii. Roasti
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A.2.3.5 A.2.3.6 A.2.3.6.1 A.2.3.6.2
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A.2.3.6.8 A.2.3.6.9 A.2.3.6.10 A.2.
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A.3.1 Introduction CHAPTERA-3 RESUL
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Table A3-1b: The crude fat and crud
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A.3.3 Mineral analysis The composit
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.=-- I:TOFMSd I' EWM 1 1 1 .1 "'I I
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Inhibition oftrypsin obtained with
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Phytochemical screening was carried
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The phytate content of the Amadumbe
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Carbohydrates supply the most energ
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.\.4.2.2 Mineral analysis Diet is r
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determine fatty acid composition. P
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(Njintang et al., 2006), whereas ta
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owing to the adverse effects ofhigh
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Thus, it was observed that several
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The study showed that Amadumbe tube
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REFERENCES Adeparusi E.O. (2001) Ef
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Badifu G.I.O. (2001) Effect of proc
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Britton 1., Pavord 1., Richards K,
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OiffJ., Nicala D., Saute F., Givrag
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Duthie G.G., Duthie SJ. and Kyle AM
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Fook JM.S.L.L., Macedo l.L.P., Moma
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Hagerman AE. and Butler L.G. (1991)
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Huang Y.-e., Chang Y.-H. and Shao Y
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Liener I.E. (1982) Toxic constituen
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Mattila P. and Hellstrom J. (2007)
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Naczk M and Shabidi F. (2006) Pheno
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Onabolu AO., Oluwole O.SA, Bokanga
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Price, MP. and Butler L.G. (1977).
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Reddy N.R.and Pierson MD. (1994) Re
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Sasikiran KG., Padmaja e.S., Easwar
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Simeonova F.P. and Fishbein 1. (200
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Urbano G., L6pez-Jurado M, Aranda P
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World Health Organisation Consultat
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B1.1.1 Introduction CHAPTER Bl-l: a
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B1.1.2.1 Lectin-like a-amylase inhi
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a.-Amylase inhibitors could functio
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B1.2.1 Introduction B1.2.2 Material
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B1.2.3.1.1 The supernatant (designa
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The profile ofthe ion-exchange chro
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Optimum pH for amylase inlnbitor ac
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B1.4.3.2 inhibitor molecule general
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B2.1.1 B2.1.2.1 Introduction CHAPTE
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1l2.1.2.2 acetylCoA + acetoacetyl C
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82.1.2.4 or (PH sn .. (pa'MsI) Fi
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B2.2.1 B2.2.2 B2.2.3 Introduction C
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B2.2.3.3 Spectroscopy B2.2.3.3.1 In
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B2.3.t B2.3.2 Introduction CHAPfER
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Sitosterols are the most extensivel
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B.S.l a-Amylase inhibitor B.S.2 Sap
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Boivin M., Flourie B., Rizza RA, Go
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Durward S., Smith IN., Cash W-K N.
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Heidari R., Zareae S. and Heidariza
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Maskos K., Huber-Wunderlich M and G
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Osagie AU. (1977) Phytosterols in s
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Sondhia S. (2005) Isolation, struct
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Wretensjo 1. (2004) Characterisatio
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c.1.1 Introduction CHAPTERC-l LITER
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C.1.2.3 respoDSlble for transport o
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C.1.3 Cl.3.! replaces some of the c
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C.l.4 Aim and outline ofSection C T
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C.2.2.3 C.2.2.3.1 Preliminary toxic
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C.2.2A.3 C.2.2.5 C.2.2.5.1 biochemi
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C.3.2.3 C.3.3 C.3.3.1 Clinical sign
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C.3.3.4 Haematology tests Serum bio
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Animals treated with beta-sitostero
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Figure C3-6: Representative photomi
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.'" ... .., ., .... •.'" ... Figu
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of free cholesterol depends on mixe
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indicate that beta-sitosterol boost
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CHAYfERC-5 CONCLUSION C.S.! Beta-si
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Bouic P J D. (2001) The role ofphyt
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Ellsworth J.L., Erickson SK and Coo
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Kwiterovich P.O. (2000) The metabol
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Nair P., Turjman N., Kessie G., CaI
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Vasarhelyi B., Szab6 T., Vec A and
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2.3 Cbaracterization and nntritiona
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AppendixA PREPARATION OF REAGENTS A
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A.A.ll 0.1 M Orthophosphorieletbano
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Liquid surfaces were fonned with et
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water. The homogenate was filtered
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410 DID and the colour remained sta
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B.A.2.9 Alkaloid [Harborne (1973»)
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Dextran blue was used to determine
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180 = molecular weight ofthe glucos
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AppendixD CERTIFICATE FROM ETInCS C
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