Ligand-induced thermal stability in β-galactosidase from the seeds of the black bean, Kestingeilla geocarpa

Process Biochemistry

Volumn 38, Issue 2, 2002, Pages 143-149

  Chilaka, Ferdinand C ^a   Okeke, Chinedu ^a   Adaikpoh, Enwere ^a  

^a UNIVERSITY OF NIGERIA   (Nigeria)

Author keywords

Black bean; Properties; Thermal inactivation; Thermal stability; Galactosidase

Indexed keywords

PHASEOLUS (ANGIOSPERM);

EID: 0036807095     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0032-9592(01)00321-1     Document Type: Article

References (25)

1. Biswas TK. Characterization of β-galactosidase from the germinating seeds of Vigna sinensis. Phytochemistry 1987;26:359-64.
2. Sekimata M, Ogura K, Tsumuraya Y, Hashimoto Y, Yamamoto S. A β-galactosidase from Radish (Raphanus sativus L.). Plant Physiol 1989;90:567-74.
3. Bouranis DL, Niavis LA. Cell wall metabolism in growing and ripening store fruits. Plant Cell Physiol 1992;33:999-1008.
4. Ali ZM, Armugen S, Lazan H. β-Galactosidase and its significance in ripening mango fruits. Phytochemistry 1995;38:1109-14.
5. Fukuda MN, Fukuda M, Hakamori SI. Cell surface modification by endo-galactosidase. J Biol Chem 1979;254:5458-65.
6. Hibachi F, Hata J, Mitra M, Dha M, Harmata M, Sun P, Smith D. Purification and characterization of a coffee Canephora α-galactosidase enzyme. Brioche Biophys Res Commun 1991;181:180-4.
7. Oates MDG, Rosbottom AL, Sihrafer J. Further investigation into the structure of human gastric mucin. The structural configuration of the oligossaccharide chains. Carbohydr Res 1974;34:115-37.
8. Kornfeld R, Kornfeld S. Structure of glycoproteins and their oligosaccharide. In: Lennarz WJ, editor. Biochemistry of Glycoproteins and Proteoglycans. New York: Plenum Press, 1980:1-34.
9. Richmond ML, Gray JI, Stine CM. Beta-galactosidase. Review of recent research related to technological application: Nutritional concerns and immobilization. J Diary Sci 1981;64:1759-71.
10. Biswas TK. Cationic form of β-galactosidase in the germinating seeds of Vigna sinensis (Linn) Savi. Arch Biochem Biophys 1986;252:379-84.
11. Hubbard SJ. The structural aspects of limited proteolysis of native proteins. Biochim Biophys Acta 1998;1382:191-206.
12. Volkin DB, Klibanov AM. Minimizing protein inactivation. In: Creighton TE, editor. Protein Function, a Practical Approach. IRL Press Oxford University, 1989:1-54.
13. Bhasker B, Prakesh V, Savithri S, Rao AN. Interactions of L-serine at the active site of serine hydroxymethyl transferases. Induction of thermal stability. Biochem Biophy Acta 1994;1209:40-50.
14. Sasso S, Protasevich I, Gill R, Makarov A, Briand C. Thermal denaturation of bacterial and bovine dihydrofolate reductases and their complexes with NADPH, Trimethoprin and methotrexate. J Biomol Struct Dynam 1995;12:1023-32.
15. Kornilaev BA, Kurganov BI, Eronina TB, Livanona NB. Thermal inactivation of muscle phosphorylase B. Protective effect of specific ligands. Biochem Mol Biol Int 1996;38:921-7.
16. Daniel RM, Dines M, Peach HH. The denaturation and degradation of stable enzymes at high temperature. Biochem J 1996;317:1-11.
17. Lowry OH, Rosenbrough NJ, Farr AC, Randall RJ. Protein measurement with Folin-phenol reagent. J Biol Chem 1951;193:265-75.
18. Veau EJI, Gross KC, Huber DJ, Watada A. Degradation and volatilization of pectin by β-galactosidase purified from avocado mesocarp. Physiol Plant 1993;87:279-85.
19. McClellan KM, Robinson DS. The effect of heat on cabbage and Brussels sprout peroxidase enzymes. Food Chem 1981;7:257-66.
20. Yoshioka S, Aso Y, Izutsu KI, Kojima S. Is stability prediction possible for protein drugs: Denaturation kinetics of β-galactosidase in solution. Pharm Res 1994;11:1721-5.
21. Seckler R, Jaenicke R. Protein folding and protein refolding. FASEB J 1992;6:2545-52.
22. Horowitz P, Bowman S. Reversible thermal denaturation of immobilized rhodanase. J Biol Chem 1987;262:5587-91.
23. Zale SE, Klibanov AM. Mechanism of irreversible thermoinactivation of enzymes. Ann NY Acad Sci 1986;434:20-6.
24. Creighton TE. Protein folding pathways determined using disulphide bonds. Bioessays 1992;14:195-9.
25. Nimmesgen E, Fox T, Fleming MA, Thomson JA. Conformational changes and stabilization of inosine 5-monophosphate dehydrogenase associated with ligand binding and inhibition of monophenolic acid. J Biol Chem 1996;271:19421-7.