Zobrazeno 1 - 10
of 74
pro vyhledávání: '"Huei-Fen Lo"'
Autor:
Tzu-Fan Wang, Meng-Chun Chi, Kuan-Ling Lai, Min-Guan Lin, Yi-Yu Chen, Huei-Fen Lo, Long-Liu Lin
Publikováno v:
PeerJ, Vol 6, p e5863 (2018)
Long-term use of organophosphorus (OP) compounds has become an increasing global problem and a major threat to sustainability and human health. Prolidase is a proline-specific metallopeptidase that can offer an efficient option for the degradation of
Externí odkaz:
https://doaj.org/article/db113e87514b4721b3ae49caabf0bef1
Publikováno v:
Biomolecules, Vol 9, Iss 9, p 508 (2019)
A highly conserved 458PLSSMXP464 sequence in the small subunit (S-subunit) of an industrially important Bacillus licheniformis γ-glutamyltranspeptidase (BlGGT) was identified by sequence alignment. Molecular structures of the precursor mimic and the
Externí odkaz:
https://doaj.org/article/1e44b96b74204b03a3f49dec21cbe657
Autor:
Huei-Fen Lo, 羅蕙芬
91
α-Amylase is an endo-type enzyme that hydrolyses internal glucosidic linkage on the starch backbone. It is used extensively in the bioprocessing of starch to produce various sugar syrups. Theα-amylase gene of Bacillus sp. strain TS-23 consi
α-Amylase is an endo-type enzyme that hydrolyses internal glucosidic linkage on the starch backbone. It is used extensively in the bioprocessing of starch to produce various sugar syrups. Theα-amylase gene of Bacillus sp. strain TS-23 consi
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/dmk4dm
Publikováno v:
Journal of Microbiology and Biotechnology. 28:1457-1466
In the present study, the stabilizing effect of four different biological osmolytes on Bacillus licheniformis γ-glutamyl transpeptidase (BlGGT) was investigated. BlGGT appeared to be stable under temperatures below 40°C, but the enzyme retained les
Publikováno v:
Biocatalysis and Agricultural Biotechnology. 10:278-284
Several γ-glutamyl compounds are known to have attractive features for food industry applications. In this study, we report a straightforward procedure for the biocatalytic synthesis of γ-glutamyl-phenylalanine (γ-Glu-Phe) using recombinant Bacill
Protective Effect of Biological Osmolytes against Heat- and Chaotropic Agent-Induced Denaturation of
Publikováno v:
Journal of microbiology and biotechnology. 28(9)
In the present study, the stabilizing effect of four different biological osmolytes on
Autor:
Huei-Fen Lo, Kuan-Ling Lai, Min-Guan Lin, Long-Liu Lin, Tzu-Fan Wang, Yi-Yu Chen, Meng-Chun Chi
Publikováno v:
PeerJ, Vol 6, p e5863 (2018)
Long-term use of organophosphorus (OP) compounds has become an increasing global problem and a major threat to sustainability and human health. Prolidase is a proline-specific metallopeptidase that can offer an efficient option for the degradation of
Publikováno v:
Biomolecules
Biomolecules, Vol 9, Iss 9, p 508 (2019)
Volume 9
Issue 9
Biomolecules, Vol 9, Iss 9, p 508 (2019)
Volume 9
Issue 9
A highly conserved 458PLSSMXP464 sequence in the small subunit (S-subunit) of an industrially important Bacillus licheniformis &gamma
glutamyltranspeptidase (BlGGT) was identified by sequence alignment. Molecular structures of the precursor mimi
glutamyltranspeptidase (BlGGT) was identified by sequence alignment. Molecular structures of the precursor mimi
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 15, p 3625 (2019)
International Journal of Molecular Sciences
Volume 20
Issue 15
International Journal of Molecular Sciences
Volume 20
Issue 15
In this study, silica-coated magnetic nanoparticles (SiMNPs) with isocyanatopropyltriethoxysilane as a metal-chelating ligand were prepared for the immobilization of His6-tagged Escherichia coli prolidase (His6-EcPepQ). Under one-hour coupling, the e
Autor:
Den-Tai Lin, Long-Liu Lin, Huei-Fen Lo, Yen-Chung Lee, Hui-Yu Hu, Hsiao Nai-Wan, Hsiang-Ling Chen
Publikováno v:
Protein & Peptide Letters. 19:1183-1193
The NAD(+)-requiring enzymes of the aldehyde dehydrogenase (ALDH) family contain a glycine motif, GX1- 2GXXG, which is reminiscent of the fingerprint region of the Rossman fold, a conserved structural motif of the classical nicotinamide nucleotide-bi