Simultaneous enhanced catalytic activity and thermostability of a 1,3-1,4-β-glucanase from Bacillus amyloliqueformis by chemical modification of lysine residues

Biotechnology Letters

Volumn 36, Issue 12, 2014, Pages 2453-2460

  Niu, Chengtuo ^a   Zhu, Linjiang ^a   Wang, Jinjing ^a   Li, Qi ^a  

^a JIANGNAN UNIVERSITY   (China)

Author keywords

1,3 1,4 Glucanase; Bacillus amyloliquefaciens; Catalytic activity; Chemical modification; Lysine residues; Nitrous acid; Thermostability

Indexed keywords

AMINO ACIDS; BACTERIOLOGY; CHEMICAL MODIFICATION; DICHROISM; INORGANIC ACIDS; STABILITY;

BACILLUS AMYLOLIQUEFACIENS; GLUCANASE; LYSINE RESIDUES; NITROUS ACID; THERMOSTABILITY;

CATALYST ACTIVITY;

BACILLUS AMYLOLIQUEFACIENS;

GLYCOSIDASE; LICHENINASE; LYSINE; NITROUS ACID;

BACILLUS; CHEMISTRY; CIRCULAR DICHROISM; ENZYME STABILITY; ENZYMOLOGY; GENETICS; METABOLISM; PROTEIN PROCESSING; PROTEIN STABILITY; RADIATION RESPONSE; TEMPERATURE; TIME;

BACILLUS; CIRCULAR DICHROISM; ENZYME STABILITY; GLYCOSIDE HYDROLASES; LYSINE; NITROUS ACID; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STABILITY; TEMPERATURE; TIME FACTORS;

EID: 84911983259     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-014-1616-0     Document Type: Article

References (18)

1. Cornelis P, Digneffe C, Willemot K (1982) Cloning and expression of a Bacillus coagulans amylase gene in Escherichia coli. Mol Gen Genet 186:507–511
2. Etter M (1990) Encoding and decoding hydrogen-bond patterns of organic compounds. Acc Chem Res 23:120–126
3. Fields PA (2001) Review: protein function at thermal extremes: balancing stability and flexibility. Comp Biochem Physiol A 129:417–431
4. Garrett GH, Grisham CM (1999) Biochemistry, 2nd edn. Saunders College Publishing, Fort Worth
5. Greenwood N, Earnshaw A (1997) Chemistry of the elements, 2nd edn. Elsevier Butterworth-Heinemann Publishing, Oxford
6. Hahn M, Pons J, Planas A, Querol E, Heinemann U (1995) Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution. FEBS Lett 374:221–224
7. Hofemeister J, Kurtz A, Borriss R, Knowles J (1986) The beta-glucanase gene from Bacillus amyloliquefaciens shows extensive homology with that of Bacillus subtilis. Gene 49:177–187
8. Khajeh K, Naderi-Manesh H, Ranjbar B, Moosavi-Movahedi A, Nemat-Gorgani M (2001) Chemical modification of lysine residues in Bacillus alpha-amylases: effect on activity and stability. Enz Microb Technol 28:543–549
9. Li Y, Xie Y, Zhu L, Zhang Y, Gu G, Li Q (2009) Optimization of cloning and expression of beta-glucanase gene from Bacillus amyloliquefaciens. Chin J Biotech 25:542–548
10. Pack SP, Yoo YJ (2004) Protein thermostability: structure-based difference of amino acid between thermophilic and mesophilic proteins. J Biotechnol 111:269–277
11. Planas A (2000) Bacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering. Biochim Biophys Acta 1543:361–382
12. Quintanilla-Guerrero F, Duarte-Vazquez MA, Tinoco R, Gomez-Suarez M, Garcia-Almendarez BE, Vazquez-Duhalt R, Regalado C (2008) Chemical modification of turnip peroxidase with methoxypolyethylene glycol enhances activity and stability for phenol removal using the immobilized enzyme. J Agric Food Chem 56:8058–8065
13. Rother K, Hildebrand PW, Goede A, Gruening B, Preissner R (2009) Voronoia: analyzing packing in protein structures. Nucleic Acids Res 37:393–395
14. Schimming S, Schwarz WH, Staudenbauer WL (1991) Properties of a thermoactive beta-1,3-1,4-glucanase (lichenase) from Clostridium thermocellum expressed in Escherichia coli. Biochem Biophys Res Commun 177:447–452
15. Sterpone F, Stirnemann G, Hynes J, Laage D (2010) Water hydrogen-bond dynamics around amino acids: the key role of hydrophilic hydrogen-bond acceptor groups. J Phys Chem 114:2083–2089
16. Vriend G (1990) WHAT IF: a molecular modeling and drug design program. J Mol Graph 8:52–56
17. Wang J, Niu C, Liu X, Chen X, Li Q (2014) Characterization of a new 1,3-1,4-beta-glucanase gene from Bacillus tequilensis CGX5-1. Appl Biochem Biotechnol. doi:10.1007/s12010-014-0900-8
18. Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89:392–400