Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology

The enzymatic condition for producing the anti-obesity hydrolysates from fish water-soluble protein was optimized with the aid of response surface methodology, which also derived a statistical model for experimental validation. Compared with neutral protease, papain and protamex, the porcine pancrea...
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Autor*in:	Jinju Wang [verfasserIn] Chen Peng [verfasserIn] Yanping Wang [verfasserIn] Liyuan Liu [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2013

Schlagwörter:	anti-obesity fish protein kinetics porcine pancreas lipase α-amylase response surface methodology (RSM)

Übergeordnetes Werk:	In: International Journal of Molecular Sciences - MDPI AG, 2003, 14(2013), 2, Seite 3124-3139
Übergeordnetes Werk:	volume:14 ; year:2013 ; number:2 ; pages:3124-3139

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/ijms14023124

Katalog-ID:	DOAJ077664620

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520			\|a The enzymatic condition for producing the anti-obesity hydrolysates from fish water-soluble protein was optimized with the aid of response surface methodology, which also derived a statistical model for experimental validation. Compared with neutral protease, papain and protamex, the porcine pancreas lipase inhibitory rate of hydrolysates from fish water-soluble protein was higher with alkaline protease. Results showed that the model terms were significant, the terms of lack of fit were not significant, and the optimal conditions for the hydrolysis by alkaline protease were initial pH 11, temperature 39 °C, enzyme dosage 122 U/mL and 10 h of hydrolysis time. Under these conditions, the porcine pancreas lipase and the α-amylase inhibitory rate could reach 53.04% ± 1.32% and 20.03 ± 0.89%, while predicted value were 54.63% ± 1.75%, 21.22% ± 0.70%, respectively. In addition, Lineweaver-Burk plots showed noncompetitive inhibition. The Ki value calculated was 84.13 mg/mL. These results demonstrated that fish water-soluble protein could be used for obtaining anti-obesity hydrolysates.
650		4	\|a anti-obesity
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allfields	10.3390/ijms14023124 doi (DE-627)DOAJ077664620 (DE-599)DOAJ9f55ef36ff104dc5aea2c5a6ba1ec233 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Jinju Wang verfasserin aut Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The enzymatic condition for producing the anti-obesity hydrolysates from fish water-soluble protein was optimized with the aid of response surface methodology, which also derived a statistical model for experimental validation. Compared with neutral protease, papain and protamex, the porcine pancreas lipase inhibitory rate of hydrolysates from fish water-soluble protein was higher with alkaline protease. Results showed that the model terms were significant, the terms of lack of fit were not significant, and the optimal conditions for the hydrolysis by alkaline protease were initial pH 11, temperature 39 °C, enzyme dosage 122 U/mL and 10 h of hydrolysis time. Under these conditions, the porcine pancreas lipase and the α-amylase inhibitory rate could reach 53.04% ± 1.32% and 20.03 ± 0.89%, while predicted value were 54.63% ± 1.75%, 21.22% ± 0.70%, respectively. In addition, Lineweaver-Burk plots showed noncompetitive inhibition. The Ki value calculated was 84.13 mg/mL. These results demonstrated that fish water-soluble protein could be used for obtaining anti-obesity hydrolysates. anti-obesity fish protein kinetics porcine pancreas lipase α-amylase response surface methodology (RSM) Biology (General) Chemistry Chen Peng verfasserin aut Yanping Wang verfasserin aut Liyuan Liu verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 14(2013), 2, Seite 3124-3139 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:14 year:2013 number:2 pages:3124-3139 https://doi.org/10.3390/ijms14023124 kostenfrei https://doaj.org/article/9f55ef36ff104dc5aea2c5a6ba1ec233 kostenfrei http://www.mdpi.com/1422-0067/14/2/3124 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 14 2013 2 3124-3139
spelling	10.3390/ijms14023124 doi (DE-627)DOAJ077664620 (DE-599)DOAJ9f55ef36ff104dc5aea2c5a6ba1ec233 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Jinju Wang verfasserin aut Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The enzymatic condition for producing the anti-obesity hydrolysates from fish water-soluble protein was optimized with the aid of response surface methodology, which also derived a statistical model for experimental validation. Compared with neutral protease, papain and protamex, the porcine pancreas lipase inhibitory rate of hydrolysates from fish water-soluble protein was higher with alkaline protease. Results showed that the model terms were significant, the terms of lack of fit were not significant, and the optimal conditions for the hydrolysis by alkaline protease were initial pH 11, temperature 39 °C, enzyme dosage 122 U/mL and 10 h of hydrolysis time. Under these conditions, the porcine pancreas lipase and the α-amylase inhibitory rate could reach 53.04% ± 1.32% and 20.03 ± 0.89%, while predicted value were 54.63% ± 1.75%, 21.22% ± 0.70%, respectively. In addition, Lineweaver-Burk plots showed noncompetitive inhibition. The Ki value calculated was 84.13 mg/mL. These results demonstrated that fish water-soluble protein could be used for obtaining anti-obesity hydrolysates. anti-obesity fish protein kinetics porcine pancreas lipase α-amylase response surface methodology (RSM) Biology (General) Chemistry Chen Peng verfasserin aut Yanping Wang verfasserin aut Liyuan Liu verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 14(2013), 2, Seite 3124-3139 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:14 year:2013 number:2 pages:3124-3139 https://doi.org/10.3390/ijms14023124 kostenfrei https://doaj.org/article/9f55ef36ff104dc5aea2c5a6ba1ec233 kostenfrei http://www.mdpi.com/1422-0067/14/2/3124 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 14 2013 2 3124-3139
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allfieldsSound	10.3390/ijms14023124 doi (DE-627)DOAJ077664620 (DE-599)DOAJ9f55ef36ff104dc5aea2c5a6ba1ec233 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Jinju Wang verfasserin aut Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The enzymatic condition for producing the anti-obesity hydrolysates from fish water-soluble protein was optimized with the aid of response surface methodology, which also derived a statistical model for experimental validation. Compared with neutral protease, papain and protamex, the porcine pancreas lipase inhibitory rate of hydrolysates from fish water-soluble protein was higher with alkaline protease. Results showed that the model terms were significant, the terms of lack of fit were not significant, and the optimal conditions for the hydrolysis by alkaline protease were initial pH 11, temperature 39 °C, enzyme dosage 122 U/mL and 10 h of hydrolysis time. Under these conditions, the porcine pancreas lipase and the α-amylase inhibitory rate could reach 53.04% ± 1.32% and 20.03 ± 0.89%, while predicted value were 54.63% ± 1.75%, 21.22% ± 0.70%, respectively. In addition, Lineweaver-Burk plots showed noncompetitive inhibition. The Ki value calculated was 84.13 mg/mL. These results demonstrated that fish water-soluble protein could be used for obtaining anti-obesity hydrolysates. anti-obesity fish protein kinetics porcine pancreas lipase α-amylase response surface methodology (RSM) Biology (General) Chemistry Chen Peng verfasserin aut Yanping Wang verfasserin aut Liyuan Liu verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 14(2013), 2, Seite 3124-3139 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:14 year:2013 number:2 pages:3124-3139 https://doi.org/10.3390/ijms14023124 kostenfrei https://doaj.org/article/9f55ef36ff104dc5aea2c5a6ba1ec233 kostenfrei http://www.mdpi.com/1422-0067/14/2/3124 kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 14 2013 2 3124-3139
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callnumber-first	Q - Science
author	Jinju Wang
spellingShingle	Jinju Wang misc QH301-705.5 misc QD1-999 misc anti-obesity misc fish protein misc kinetics misc porcine pancreas lipase misc α-amylase misc response surface methodology (RSM) misc Biology (General) misc Chemistry Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology
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topic_title	QH301-705.5 QD1-999 Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology anti-obesity fish protein kinetics porcine pancreas lipase α-amylase response surface methodology (RSM)
topic	misc QH301-705.5 misc QD1-999 misc anti-obesity misc fish protein misc kinetics misc porcine pancreas lipase misc α-amylase misc response surface methodology (RSM) misc Biology (General) misc Chemistry
topic_unstemmed	misc QH301-705.5 misc QD1-999 misc anti-obesity misc fish protein misc kinetics misc porcine pancreas lipase misc α-amylase misc response surface methodology (RSM) misc Biology (General) misc Chemistry
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title	Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology
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title_full	Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology
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title_sort	optimization of the preparation of fish protein anti-obesity hydrolysates using response surface methodology
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title_auth	Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology
abstract	The enzymatic condition for producing the anti-obesity hydrolysates from fish water-soluble protein was optimized with the aid of response surface methodology, which also derived a statistical model for experimental validation. Compared with neutral protease, papain and protamex, the porcine pancreas lipase inhibitory rate of hydrolysates from fish water-soluble protein was higher with alkaline protease. Results showed that the model terms were significant, the terms of lack of fit were not significant, and the optimal conditions for the hydrolysis by alkaline protease were initial pH 11, temperature 39 °C, enzyme dosage 122 U/mL and 10 h of hydrolysis time. Under these conditions, the porcine pancreas lipase and the α-amylase inhibitory rate could reach 53.04% ± 1.32% and 20.03 ± 0.89%, while predicted value were 54.63% ± 1.75%, 21.22% ± 0.70%, respectively. In addition, Lineweaver-Burk plots showed noncompetitive inhibition. The Ki value calculated was 84.13 mg/mL. These results demonstrated that fish water-soluble protein could be used for obtaining anti-obesity hydrolysates.
abstractGer	The enzymatic condition for producing the anti-obesity hydrolysates from fish water-soluble protein was optimized with the aid of response surface methodology, which also derived a statistical model for experimental validation. Compared with neutral protease, papain and protamex, the porcine pancreas lipase inhibitory rate of hydrolysates from fish water-soluble protein was higher with alkaline protease. Results showed that the model terms were significant, the terms of lack of fit were not significant, and the optimal conditions for the hydrolysis by alkaline protease were initial pH 11, temperature 39 °C, enzyme dosage 122 U/mL and 10 h of hydrolysis time. Under these conditions, the porcine pancreas lipase and the α-amylase inhibitory rate could reach 53.04% ± 1.32% and 20.03 ± 0.89%, while predicted value were 54.63% ± 1.75%, 21.22% ± 0.70%, respectively. In addition, Lineweaver-Burk plots showed noncompetitive inhibition. The Ki value calculated was 84.13 mg/mL. These results demonstrated that fish water-soluble protein could be used for obtaining anti-obesity hydrolysates.
abstract_unstemmed	The enzymatic condition for producing the anti-obesity hydrolysates from fish water-soluble protein was optimized with the aid of response surface methodology, which also derived a statistical model for experimental validation. Compared with neutral protease, papain and protamex, the porcine pancreas lipase inhibitory rate of hydrolysates from fish water-soluble protein was higher with alkaline protease. Results showed that the model terms were significant, the terms of lack of fit were not significant, and the optimal conditions for the hydrolysis by alkaline protease were initial pH 11, temperature 39 °C, enzyme dosage 122 U/mL and 10 h of hydrolysis time. Under these conditions, the porcine pancreas lipase and the α-amylase inhibitory rate could reach 53.04% ± 1.32% and 20.03 ± 0.89%, while predicted value were 54.63% ± 1.75%, 21.22% ± 0.70%, respectively. In addition, Lineweaver-Burk plots showed noncompetitive inhibition. The Ki value calculated was 84.13 mg/mL. These results demonstrated that fish water-soluble protein could be used for obtaining anti-obesity hydrolysates.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
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title_short	Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology
url	https://doi.org/10.3390/ijms14023124 https://doaj.org/article/9f55ef36ff104dc5aea2c5a6ba1ec233 http://www.mdpi.com/1422-0067/14/2/3124 https://doaj.org/toc/1422-0067
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Optimization of the Preparation of Fish Protein Anti-Obesity Hydrolysates Using Response Surface Methodology

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