Chimeric ß-glucosidase between Cellvibrio gilvus and Ruminococcus albus enzymes

Autor:	Kiyoshi Hayashi, Ajay Singh, Truong Thi Hoa, Chika Aoyagi, Kunio Ohmiya, Kenji Iwakiri, Ken Tokuyasu
Jazyk:	angličtina
Rok vydání:	1999
Předmět:	chemistry.chemical_classification animal structures Multidisciplinary lcsh:Biotechnology Chimeric enzyme Heat stability Cellvibrio gilvus Biology Ruminococcus albus Homology (biology) Enzyme assay Amino acid Enzyme chemistry Biochemistry lcsh:TP248.13-248.65 biology.protein ß-glucosidase Chimeric
Zdroj:	Brazilian Archives of Biology and Technology, Volume: 42, Issue: 3, Pages: 303-306, Published: 1999 Brazilian Archives of Biology and Technology, Vol 42, Iss 3, Pp 303-306 (1999) Brazilian Archives of Biology and Technology v.42 n.3 1999 Brazilian Archives of Biology and Technology Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR
Popis:	Based on homology search in the amino acid sequences, a chimeric ß-glucosidase with enzyme activity has been prepared by replacing C-terminal region of Thr509-Arg646 from Cellvibrio gilvus with N-terminal region of Arg160-Gly283 from Ruminococcus albus. The chimeric enzyme showed broader optimum pH and slightly higher heat stability compared with original C. gilvus enzyme.Baseado na busca de homólogos na seqüência de aminoácidos, uma ß glucosidase - quimérica com atividade enzimática foi preparada para substituir C-terminal na região de Thr509-Arg646 de Cellvibrio gilvus com N-terminal na região de Arg160-Gly283 de Ruminococcus albus. A enzima quimérica mostrou pH ótimo mais amplo e estabilidade levemente mais alta ao calor comparada com a enzima original de C. gilvus.
Databáze:	OpenAIRE
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