Comparative Analysis of Β- Glucosidases Thermostability: Differences in Amino Acids Composition and Distribution among Mesostable and Thermostable Β- Glucosidases
نویسندگان
چکیده
Out of various industrial enzymes, thermostable βglucosidases are of great interest, due to their utility in conversion of lingocellulosic material into bioethanol. Determination of the factors responsible for thermostability in β-glucosidases by sequence and structure comparison will be useful in identification, isolation and design of novel thermostable βglucosidases. In the present study thermostable and mesostable β-glucosidases sequences retrieved from Uniport database were subjected to in-silico physio-chemical characterisation, multiple sequence alignment, phylogenetic tree construction and motif prediction using various bioinformatic tools. Present study revealed that thermostable βglucosidases and mesophillic βglucosidases are similar in percentage amino acids composition, share physico-chemical characteristics and secondary structures. But thermostable βglucosidases have low GRAVY value, low percentage of glutamine (hydrophilic amino acid), conserved amino acids Phenylalanine (Phe)86, Proline (Pro) – 87, 282, 396, Glutamic Acid (Glu) -102, Asparatic acid (Asp)-147, 193, 633, Tryptophan (Trp) – 222, 261, 631, 722 , Glycine (Gly) 126, 174, 255, 524, 604, 622, Leucine (leu) – 321 and Tyrosine (Tyr)605) along with 8 signature amino acid sequences that are absent in the mesophillic βglucosidases. Out of 8 motifs, one conserved motif having sequence (WG[VT][AM][TC][AS][SY][YN][QK][IL][EN]G[AE][YV][CN][ES][DE][GN]R[GT][LP]) was 100 % conserved in thermostable βglucosidases analysed in the present study.
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Characterization of a thermostable β-glucosidase from Aspergillus fumigatus Z5, and its functional expression in Pichia pastoris X33
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