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Caption: Figure 1: Infrared spectra of (a) (A) pristine L-alanine, (B) L-alanine-capped ZnS nanoparticles, and (C) L-alanine-capped CuS nanoparticles and (b) (A) pristine L-aspartic acid, (B) L-aspartic acid-capped ZnS nanoparticles, and (C) L-aspartic acid-capped CuS nanoparticles.
The existence of D-isomers may be explained by racemization [22] of L-aspartic acid or epimerization of L-aspartyl residues in the polypeptides.
The chloroacetyl chloride products of L-aspartic acid dimethyl ester (0.10 g, 0.621 mmol) as well as genistein (0.20 g, 0.740 mmol), [K.sub.2]C[O.sub.3] (0.40 g, 2.894 mmol), and KI (0.12 g, 0.723 mmol) were dissolved in DMF (10.00 mL) and reacted for 4 h at 5060[degrees]C.
In addition, it had high activities to broad L-amino acids but not to L-aspartic acid. Therefore, B3-LAAO probably presents a novel LAAO, which can enrich our knowledge on LAAO from Pseudoalteromonas genus.
While most of our strains (60-78%) were still positive and 18-28% were weakly positive to melibiose, monomethyl succinate, D-alanine, L-alanine, L-alanyl-glycine, and glycerol, only some were positive to glycyl-L-glutamic acid (41% strongly and 30% weakly), cisaconitic acid (20% strongly and 36% weakly), lactic acid (17% strongly and 50% weakly), L-proline (14% strongly and 21% weakly), L-aspartic acid (27% strongly and 23% weakly), hydroxy L-proline (34% strongly and 31% weakly), and glucose-6-phosphate (33% strongly and 36% weakly), and the reaction to [beta]-methyl D-glucoside and inosine was predominantly negative and positive with only 1% and 3% of the strains, respectively.
Asparaginase is the enzyme that hydrolyzes asparagine into L-aspartic acid and ammonia.