Crosslinking of glucoamylases via carbohydrates hardly affects catalysis but impairs stability

Biotechnology and Bioengineering

Volumn 63, Issue 4, 1999, Pages 459-463

  Sasvári, Zsuzsanna ^a   Asbóth, Bence ^a  

^a SZENT ISTVÁN UNIVERSITY   (Hungary)

Author keywords

Covalent enzyme oligomers; Crosslinking; Glucoamylase; Thermostability

Indexed keywords

CATALYSIS; CATALYST ACTIVITY; CROSSLINKING; ELECTRON MICROSCOPY; FUNGI; MALTOSE; OLIGOMERS; OXIDATION; SIZE EXCLUSION CHROMATOGRAPHY; STARCH; THERMODYNAMIC STABILITY;

GLUCOAMYLASE; PERIODATE;

ENZYMES;

ADIPIC ACID; GLUCAN 1,4 ALPHA GLUCOSIDASE; PERIODATE; TETRAMER;

ARTICLE; ASPERGILLUS NIGER; CATALYSIS; COVALENT BOND; ENZYME INACTIVATION; GEL PERMEATION CHROMATOGRAPHY; PROTEIN CROSS LINKING; THERMOSTABILITY; TRANSMISSION ELECTRON MICROSCOPY;

ASPERGILLUS NIGER; FUNGI;

EID: 0345471833     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19990520)63:4<459::AID-BIT9>3.0.CO;2-I     Document Type: Article

References (15)

1. Aleshin A, Golubev A, Firsov LM, Honzatko R. 1992. Crystal Structure of Glucoamylase from Aspergillus awamori var. X100 to 2.2-Å Resolution. J Biol Chem 267:19291-19298.
2. Back JF, Oakenfull D, Smith MB. 1979. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry 18:5191-5196.
3. Cesi V. 1992. Stabilization of glycoenzyme acid phosphatase by crosslinking of its carbohydrate chains. In: Steiner W and Haltrich D, editors. Conference on Biotechnology in Central European Initiative Countries. Graz, Austria. Vienna: Federal Ministry for Science and Research, p 139.
4. Chen HM, Li Y, Panda T, Buehler FU, Ford C, Reilly PJ. 1996. Effect of replacing helical glycine residues with alanines on reversible and irreversible stability and production of Aspergillus awamori glucoamylase. Prot Eng 9:499-505.
5. Clarke AJ, Svensson B. 1984. The role of tryptophanyl residues in the function of Aspergillus niger glucoamylase G1 and G2. Carlsberg Res Commun 49:111-122.
6. Coutinho PM, Reilly PJ. 1997. Glucoamylase structural, functional and evolutionary relationships. Proteins 29:334-347.
7. Gunnarson A, Svensson B, Nilsson B, Svensson S. 1984. Structural studies on the O-glycosidically linked carbohydrate chains of glucoamylase G1 from Aspergillus niger. Eur J Biochem 145:463-468.
8. Kozulic B. Barbaric S, Ries S, Mildner P. 1984. Study of the carbohydrate part of yeast acid phosphatase. Biochem Biophys Res Commun 122:1083-1087.
9. Kozulic B, Leustek I, Pavlovic B, Mildner P, Barbaric S. 1987. Preparation of the stabilized glycoenzymes by cross-linking their carbohydrate chains. Appl Biochem Biotechnol 15:265-278.
10. Kramer GHF, Gunning AP, Morris VJ, Belshaw NJ, Williamson G. 1993. Scanning Tunneling Microscopy of Aspergillus niger Glucoamylase. J Chem Soc Faraday Trans 89:2595-2602.
11. Libby CB, Cornett CAG, Reilly PJ, Ford C. 1994. Effect of amino acid deletions in the O-glycosylated region of Aspergillus awamori glucoamylase. Prot Eng 7:1109-1114.
12. Sasvári Z, Asbóth B. 1998. Formation of disulfide-bridged dimers during thermoinactivation of glucoamylase from Aspergillus niger Enzyme Microb Technol 22:466-470.
13. Van Lenten L, Ashwell G. 1971. Studies on the chemical and enzymatic modification of glycoproteins. A general method for the titration of sialic acid-containing. J Biol Chem 246:1889-1894.
14. Várallyay E, Sasvári Z, Hoschke A, Asbóth B. 1994. A potential protein engineering site in Aspergillus niger glucoamylase: vicinity of disulphide bridge 449-222. Acta Alimentaria 23:93-103.
15. Williamson G, Belshaw NJ, Noel TR, Ring SG, Williamson MP. O-glycosylation and stability. Unfolding of glucoamylase induced by heat and guanidine hydrocloride. 1992. Eur J Biochem 207:661-670.