Cargando…
Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223
Experiments were carried out to investigate the effects of various factors on the activity and conformation of recombinant leucine aminopeptidase of Bacillus kaustophilus CCRC 11223 (BkLAP) and potential utilization of BkLAP in the hydrolysis of anchovy protein. Optimal temperature and pH of BkLAP w...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3233426/ https://www.ncbi.nlm.nih.gov/pubmed/22174620 http://dx.doi.org/10.3390/ijms12117609 |
_version_ | 1782218405898616832 |
---|---|
author | Shen, Yanfei Wang, Fanghua Lan, Dongming Liu, Yuanyuan Yang, Bo Wang, Yonghua |
author_facet | Shen, Yanfei Wang, Fanghua Lan, Dongming Liu, Yuanyuan Yang, Bo Wang, Yonghua |
author_sort | Shen, Yanfei |
collection | PubMed |
description | Experiments were carried out to investigate the effects of various factors on the activity and conformation of recombinant leucine aminopeptidase of Bacillus kaustophilus CCRC 11223 (BkLAP) and potential utilization of BkLAP in the hydrolysis of anchovy protein. Optimal temperature and pH of BkLAP were 70 °C and 8.0 in potassium-phosphate buffer, respectively, and the activity was strongly stimulated by Ni(2+), followed by Mn(2+) and Co(2+). Conformational studies via circular dichroism spectroscopy indicated that various factors could influence the secondary structure of BkLAP to different extents and further induce the changes in enzymatic activity. The secondary structure of BkLAP was slightly modified by Ni(2+) at the concentration of 1×10(−4) M, however, significant changes on the secondary structures of the enzyme were observed when Hg(2+) was added to the concentration of 1×10(−4) M. The potential application of BkLAP was evaluated through combination with the commercial or endogenous enzyme to hydrolysis the anchovy protein. Results showed that combining the BkLAP with other enzymes could significantly increase the degree of hydrolysis and amino acid component of hydrolysate. In this regard, BkLAP is a potential enzyme that can be used in the protein hydrolysate industry. |
format | Online Article Text |
id | pubmed-3233426 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-32334262011-12-15 Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223 Shen, Yanfei Wang, Fanghua Lan, Dongming Liu, Yuanyuan Yang, Bo Wang, Yonghua Int J Mol Sci Article Experiments were carried out to investigate the effects of various factors on the activity and conformation of recombinant leucine aminopeptidase of Bacillus kaustophilus CCRC 11223 (BkLAP) and potential utilization of BkLAP in the hydrolysis of anchovy protein. Optimal temperature and pH of BkLAP were 70 °C and 8.0 in potassium-phosphate buffer, respectively, and the activity was strongly stimulated by Ni(2+), followed by Mn(2+) and Co(2+). Conformational studies via circular dichroism spectroscopy indicated that various factors could influence the secondary structure of BkLAP to different extents and further induce the changes in enzymatic activity. The secondary structure of BkLAP was slightly modified by Ni(2+) at the concentration of 1×10(−4) M, however, significant changes on the secondary structures of the enzyme were observed when Hg(2+) was added to the concentration of 1×10(−4) M. The potential application of BkLAP was evaluated through combination with the commercial or endogenous enzyme to hydrolysis the anchovy protein. Results showed that combining the BkLAP with other enzymes could significantly increase the degree of hydrolysis and amino acid component of hydrolysate. In this regard, BkLAP is a potential enzyme that can be used in the protein hydrolysate industry. Molecular Diversity Preservation International (MDPI) 2011-11-07 /pmc/articles/PMC3233426/ /pubmed/22174620 http://dx.doi.org/10.3390/ijms12117609 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Shen, Yanfei Wang, Fanghua Lan, Dongming Liu, Yuanyuan Yang, Bo Wang, Yonghua Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223 |
title | Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223 |
title_full | Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223 |
title_fullStr | Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223 |
title_full_unstemmed | Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223 |
title_short | Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223 |
title_sort | biochemical properties and potential applications of recombinant leucine aminopeptidase from bacillus kaustophilus ccrc 11223 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3233426/ https://www.ncbi.nlm.nih.gov/pubmed/22174620 http://dx.doi.org/10.3390/ijms12117609 |
work_keys_str_mv | AT shenyanfei biochemicalpropertiesandpotentialapplicationsofrecombinantleucineaminopeptidasefrombacilluskaustophilusccrc11223 AT wangfanghua biochemicalpropertiesandpotentialapplicationsofrecombinantleucineaminopeptidasefrombacilluskaustophilusccrc11223 AT landongming biochemicalpropertiesandpotentialapplicationsofrecombinantleucineaminopeptidasefrombacilluskaustophilusccrc11223 AT liuyuanyuan biochemicalpropertiesandpotentialapplicationsofrecombinantleucineaminopeptidasefrombacilluskaustophilusccrc11223 AT yangbo biochemicalpropertiesandpotentialapplicationsofrecombinantleucineaminopeptidasefrombacilluskaustophilusccrc11223 AT wangyonghua biochemicalpropertiesandpotentialapplicationsofrecombinantleucineaminopeptidasefrombacilluskaustophilusccrc11223 |