Literature summary for 3.2.1.40 extracted from

Li, L.; Liao, H.; Yang, Y.; Gong, J.; Liu, J.; Jiang, Z.; Zhu, Y.; Xiao, A.; Ni, H.
Improving the thermostability by introduction of arginines on the surface of alpha-L-rhamnosidase (r-Rha1) from Aspergillus niger (2018), Int. J. Biol. Macromol., 112, 14-21 .

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Application

Application	Comment	Organism
food industry	with the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry	Aspergillus niger

Protein Variants

Protein Variants	Comment	Organism
K406R/K573R	to improve the thermostability of the enzyme multiple arginine residues are introduced into the r-Rha1 sequence to replace several lysine residues that located on the surface of the folded enzyme. Hinted by in silico analysis, five surface Lys residues (K134, K228, K406, K440, K573) are targeted to produce a list of 5 single-residue mutants and 4 multiple-residue mutants using site-directed mutagenesis. Among these mutants, K406R/K573R shows the best thermostability improvement. The half-life of this mutant's enzyme activity increased 3 h at 60°C, 23 min at 65°C, and 3.5 min at 70°C, when compared with the wild type. With the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry	Aspergillus niger

Organism

Organism	UniProt	Comment	Textmining
Aspergillus niger	R9W5L0	-	-
Aspergillus niger JMU-TS528	R9W5L0	-	-

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Release 2023.1 (January 2023)