BioChem - DOS

Efficient preparation of enantiopure D-phenylalanine through asymmetric resolution using immobilized phenylalanine ammonia-lyase from Rhodotorula glutinis JN-1 in a recirculating packed-bed reactor

PloS one

Zhu, Longbao; Zhou, Li; Huang, Nan; Cui, Wenjing; Liu, Zhongmei; Xiao, Ke; Zhou, Zhemin

<P>An efficient enzymatic process was developed to produce optically pure D-phenylalanine through asymmetric resolution of the racemic DL-phenylalanine using immobilized phenylalanine ammonia-lyase (<I>Rg</I>PAL) from <I>Rhodotorula glutinis</I> JN-1. <I>Rg</I>PAL was immobilized on a modified mesoporous silica support (MCM-41-NH-GA). The resulting MCM-41-NH-GA-<I>Rg</I>PAL showed high activity and stability. The resolution efficiency using MCM-41-NH-GA-<I>Rg</I>PAL in a recirculating packed-bed reactor (RPBR) was higher than that in a stirred-tank reactor. Under optimal operational conditions, the volumetric conversion rate of L-phenylalanine and the productivity of D-phenylalanine reached 96.7 mM h<SUP>&#x2212;1</SUP> and 0.32 g L<SUP>&#x2212;1</SUP> h<SUP>&#x2212;1</SUP>, respectively. The optical purity (<I>ee</I><SUB>D</SUB>) of D-phenylalanine exceeded 99%. The RPBR ran continuously for 16 batches, the conversion ratio did not decrease. The reactor was scaled up 25-fold, and the productivity of D-phenylalanine (<I>ee</I><SUB>D</SUB>>99%) in the scaled-up reactor reached 7.2 g L<SUP>&#x2212;1</SUP> h<SUP>&#x2212;1</SUP>. These results suggest that the resolution process is an alternative method to produce highly pure D-phenylalanine.</P>

2014

Public Library of Science

cc-by

1932-6203

9

9

pp.e108586

10.1371/journal.pone.0108586

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART74086453

https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0108586&type=printable