Cargando…
Optimization of Enzymatic Production of Oligopeptides from Apricot Almonds Meal with Neutrase and N120P
Neutrase 0.8L and N120P proteases were used for oligopeptide production from apricot almonds meal, and response surface design was carried out to optimize the effect of hydrolysis conditions on hydrolysis degree (DH) and oligopeptide yield rate. Four independent variables were used to optimize the h...
Autores principales: | , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3100828/ https://www.ncbi.nlm.nih.gov/pubmed/21614184 http://dx.doi.org/10.3390/ijms11124952 |
_version_ | 1782204216936235008 |
---|---|
author | Wang, Chunyan Wang, Qiang Tian, Jinqiang |
author_facet | Wang, Chunyan Wang, Qiang Tian, Jinqiang |
author_sort | Wang, Chunyan |
collection | PubMed |
description | Neutrase 0.8L and N120P proteases were used for oligopeptide production from apricot almonds meal, and response surface design was carried out to optimize the effect of hydrolysis conditions on hydrolysis degree (DH) and oligopeptide yield rate. Four independent variables were used to optimize the hydrolysis process: hydrolysis temperature (X(1)), enzyme-to substrate ratio (E/S) (X(2)), substrate concentration (X(3)) and reaction time (X(4)). Statistical analysis indicated that the four variables, quadratic terms of X(1), X(3), and X(4), and the interaction terms with X(1) had a significant (p < 0.05) effect on DH. The yield rate was also significantly affected by the four variables and quadratic terms of X(1), X(2) and X(4). Two mathematical models with high determination coefficient were obtained and could be employed to optimize protein hydrolysis. The optimal hydrolysis conditions were determined as follows: hydrolysis temperature 52.5 °C; enzyme-to-substrate ratio (E/S) 7200 U/g; substrate concentration 2%; reaction time 173 min. The initial pH 6.5 and Neutrase-to-N120P dosage ratio 2:1 were fixed in this study according to the preliminary research. Under these conditions, the experimental DH and yield rate were 34.10 ± 5.25% and 72.42 ± 2.27%, respectively. |
format | Text |
id | pubmed-3100828 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-31008282011-05-25 Optimization of Enzymatic Production of Oligopeptides from Apricot Almonds Meal with Neutrase and N120P Wang, Chunyan Wang, Qiang Tian, Jinqiang Int J Mol Sci Article Neutrase 0.8L and N120P proteases were used for oligopeptide production from apricot almonds meal, and response surface design was carried out to optimize the effect of hydrolysis conditions on hydrolysis degree (DH) and oligopeptide yield rate. Four independent variables were used to optimize the hydrolysis process: hydrolysis temperature (X(1)), enzyme-to substrate ratio (E/S) (X(2)), substrate concentration (X(3)) and reaction time (X(4)). Statistical analysis indicated that the four variables, quadratic terms of X(1), X(3), and X(4), and the interaction terms with X(1) had a significant (p < 0.05) effect on DH. The yield rate was also significantly affected by the four variables and quadratic terms of X(1), X(2) and X(4). Two mathematical models with high determination coefficient were obtained and could be employed to optimize protein hydrolysis. The optimal hydrolysis conditions were determined as follows: hydrolysis temperature 52.5 °C; enzyme-to-substrate ratio (E/S) 7200 U/g; substrate concentration 2%; reaction time 173 min. The initial pH 6.5 and Neutrase-to-N120P dosage ratio 2:1 were fixed in this study according to the preliminary research. Under these conditions, the experimental DH and yield rate were 34.10 ± 5.25% and 72.42 ± 2.27%, respectively. Molecular Diversity Preservation International (MDPI) 2010-12-02 /pmc/articles/PMC3100828/ /pubmed/21614184 http://dx.doi.org/10.3390/ijms11124952 Text en © 2010 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 Wang, Chunyan Wang, Qiang Tian, Jinqiang Optimization of Enzymatic Production of Oligopeptides from Apricot Almonds Meal with Neutrase and N120P |
title | Optimization of Enzymatic Production of Oligopeptides from Apricot Almonds Meal with Neutrase and N120P |
title_full | Optimization of Enzymatic Production of Oligopeptides from Apricot Almonds Meal with Neutrase and N120P |
title_fullStr | Optimization of Enzymatic Production of Oligopeptides from Apricot Almonds Meal with Neutrase and N120P |
title_full_unstemmed | Optimization of Enzymatic Production of Oligopeptides from Apricot Almonds Meal with Neutrase and N120P |
title_short | Optimization of Enzymatic Production of Oligopeptides from Apricot Almonds Meal with Neutrase and N120P |
title_sort | optimization of enzymatic production of oligopeptides from apricot almonds meal with neutrase and n120p |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3100828/ https://www.ncbi.nlm.nih.gov/pubmed/21614184 http://dx.doi.org/10.3390/ijms11124952 |
work_keys_str_mv | AT wangchunyan optimizationofenzymaticproductionofoligopeptidesfromapricotalmondsmealwithneutraseandn120p AT wangqiang optimizationofenzymaticproductionofoligopeptidesfromapricotalmondsmealwithneutraseandn120p AT tianjinqiang optimizationofenzymaticproductionofoligopeptidesfromapricotalmondsmealwithneutraseandn120p |