Properties of a metagenome-derived β-glucosidase from the contents of rabbit cecum

Bioscience, Biotechnology and Biochemistry

Volumn 73, Issue 7, 2009, Pages 1470-1473

  Feng, Yi ^a,b   Duan, Cheng Jie ^a   Liu, Li ^a   Tang, Ji Liang ^a   Feng, Jia Xun ^a  

^a GUANGXI UNIVERSITY   (China)

^b GUANGXI UNIVERSITY OF CHINESE MEDICINE   (China)

Author keywords

glucosidase; Characterization; Expression; Mutagenesis; Rabbit cecum

Indexed keywords

ASPARTIC ACIDS; BIOCHEMICAL PROPERTIES; CELLO-OLIGOSACCHARIDES; ENZYMATIC ACTIVITIES; EXPRESSION; GLUCOSIDASE; HIGH ACTIVITY; IN-VIVO; METAGENOMES; NATIVE ENZYMES; PH VALUE; POLYMERIZATION DEGREE; PURIFIED ENZYME; RABBIT CECUM; RECOMBINANT ENZYMES; WILD TYPES; WILD-TYPE ENZYMES;

BIOPOLYMERS; CARBOHYDRATES; ENZYMES; ESCHERICHIA COLI; MUTAGENESIS; ORGANIC ACIDS; POLYSACCHARIDES;

ENZYME ACTIVITY;

BETA GLUCOSIDASE; CHELATING AGENT; METAL; RECOMBINANT PROTEIN;

ANIMAL; ARTICLE; BIOSYNTHESIS; CATTLE; CECUM; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENE LIBRARY; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; PH; RABBIT; SITE DIRECTED MUTAGENESIS; TEMPERATURE;

ANIMALS; BETA-GLUCOSIDASE; CATTLE; CECUM; CHELATING AGENTS; ESCHERICHIA COLI; GENOMIC LIBRARY; HYDROGEN-ION CONCENTRATION; METALS; MUTAGENESIS, SITE-DIRECTED; RABBITS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TEMPERATURE;

ESCHERICHIA COLI; ORYCTOLAGUS CUNICULUS;

EID: 68649100715     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.80664     Document Type: Article

References (20)

1. Faure D, Henrissat B, Ptacek D, Bekri MA, and Vanderleyden J, Appl. Environ. Microbiol., 64, 2463-2472 (2001).
2. Zhang YHP, Himmel ME, and Mielenz JR, Biotechnol. Adv., 24, 452-481 (2006).
3. Bhatia Y, Mishra S, and Bisaria VS, Crit. Rev. Biotechnol., 22, 375-407 (2002).
4. Lin LL, Rumbak E, Zappe H, Thomson JA, and Woods DR, J. Gen. Microbiol., 136, 1567-1576 (1990).
5. Chen H, Li X, and Ljungdahl LG, Appl. Environ. Microbiol., 60, 64-70 (1994).
6. Ferrer M, Golyshina OV, Chernikova TN, Khachane AN, Reyes-Duarte D, Martins Dos Santos VAP, Strompl C, Elborough K, Jarvis G, Neef A, Yakimov MM, Timmis KN, and Golyshin PN, Environ. Microbiol., 7, 1996-2010 (2005).
7. Walter J, Mangold M, and Tannock GW, Appl. Environ. Microbiol., 71, 2347-2354 (2005).
8. Feng Y, Duan CJ, Hao P, Mo XC, Wu CF, Yu Y, Hu YL, Wei J, Tang JL, and Feng JX, Appl. Microbiol. Biotechnol., 75, 319-328 (2007).
9. Bradford MM, Anal. Biochem., 72, 248-254 (1976).
10. Laemmli UK, Nature, 224, 680-685 (1970).
11. Odoux E, Escoute J, Verdeil L, and Brillouet M, Ann. Bot., 92, 437-444 (2003).
12. Eckert K and Schneider E, Eur. J. Biochem., 270, 3593-3602 (2003).
13. Inoue T, Moriya S, Ohkuma M, and Kudo T, Gene, 349, 67-75 (2005).
14. Miller GL, Anal. Chem., 31, 426-428 (1959).
15. Pandy M and Mishra S, J. Ferment. Bioeng., 80, 446-453 (1995).
16. Ali BR, Romaniec MP, Hazlewood GP, and Freedman RB, Enzyme Microb. Technol., 17, 705-711 (1995).
17. Li YK, Chir J, and Chen FY, Biochem. J., 355, 835-840 (2001).
18. Chir J, Withers S, Wan CF, and Li YK, Biochem. J., 365, 857-863(2002).
19. Bhatia Y, Mishra S, and Bisaria VS, Biotechnol., 66, 527-535 (2005).
20. Varghese JN, Hrmova M, and Fincher GB, Structure, 7, 179-190 (1999).