Effect of processing conditions on degree of hydrolysis, ACE inhibition, and antioxidant activities of protein hydrolysate from Acetes indicus
Abstract Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using c...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Dhanabalan, Vignaesh [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag GmbH Germany 2017 |
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| Übergeordnetes Werk: |
Enthalten in: Environmental science and pollution research - Springer Berlin Heidelberg, 1994, 24(2017), 26 vom: 22. Juli, Seite 21222-21232 |
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| Übergeordnetes Werk: |
volume:24 ; year:2017 ; number:26 ; day:22 ; month:07 ; pages:21222-21232 |
| Links: |
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| DOI / URN: |
10.1007/s11356-017-9671-4 |
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OLC2040497617 |
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| 520 | |a Abstract Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using central composite design. The optimum conditions for enzyme-substrate ratio (mL/100 g) of 1.57, 1.69, 1.60, 1.56, and 1.50 and for hydrolysis time of 97.18, 96.5, 98.15 min, 102.48, and 88.44 min were established for attaining maximum yield, degree of hydrolysis, 2,2-diphenyl-1-picrylhydrazyl, angiotensin I-converting enzyme-inhibiting activity, and metal-chelating activity, respectively. ABTS radical scavenging activity and reducing power assay of optimized protein hydrolysate were found to be increased with the increase in concentration. The higher value of 7.04 (μM Trolox/g), 87.95, and 77.24%, respectively for DPPH, ACE, and metal-chelating activity indicated that the A. indicus protein hydrolysates have beneficial biological properties that could be well-utilized in the application of functional foods and nutraceuticals. Graphical abstractᅟ | ||
| 650 | 4 | |a Angiotensin I-converting enzyme | |
| 650 | 4 | |a Response surface methodology | |
| 650 | 4 | |a Degree of hydrolysis | |
| 650 | 4 | |a Reducing activity | |
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| 700 | 1 | |a Kannuchamy, Nagalakshmi |4 aut | |
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| 700 | 1 | |a Singh, Chongtham Baru |4 aut | |
| 700 | 1 | |a Balange, Amjad |4 aut | |
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10.1007/s11356-017-9671-4 doi (DE-627)OLC2040497617 (DE-He213)s11356-017-9671-4-p DE-627 ger DE-627 rakwb eng 570 360 333.7 VZ 690 333.7 540 VZ BIODIV DE-30 fid Dhanabalan, Vignaesh verfasserin aut Effect of processing conditions on degree of hydrolysis, ACE inhibition, and antioxidant activities of protein hydrolysate from Acetes indicus 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany 2017 Abstract Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using central composite design. The optimum conditions for enzyme-substrate ratio (mL/100 g) of 1.57, 1.69, 1.60, 1.56, and 1.50 and for hydrolysis time of 97.18, 96.5, 98.15 min, 102.48, and 88.44 min were established for attaining maximum yield, degree of hydrolysis, 2,2-diphenyl-1-picrylhydrazyl, angiotensin I-converting enzyme-inhibiting activity, and metal-chelating activity, respectively. ABTS radical scavenging activity and reducing power assay of optimized protein hydrolysate were found to be increased with the increase in concentration. The higher value of 7.04 (μM Trolox/g), 87.95, and 77.24%, respectively for DPPH, ACE, and metal-chelating activity indicated that the A. indicus protein hydrolysates have beneficial biological properties that could be well-utilized in the application of functional foods and nutraceuticals. Graphical abstractᅟ Angiotensin I-converting enzyme Response surface methodology Degree of hydrolysis Reducing activity Xavier, Martin (orcid)0000-0001-5879-4016 aut Kannuchamy, Nagalakshmi aut Asha, Kurukkan Kunnath aut Singh, Chongtham Baru aut Balange, Amjad aut Enthalten in Environmental science and pollution research Springer Berlin Heidelberg, 1994 24(2017), 26 vom: 22. Juli, Seite 21222-21232 (DE-627)171335805 (DE-600)1178791-0 (DE-576)038875101 0944-1344 nnns volume:24 year:2017 number:26 day:22 month:07 pages:21222-21232 https://doi.org/10.1007/s11356-017-9671-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-UMW SSG-OLC-ARC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-FOR SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4219 GBV_ILN_4277 AR 24 2017 26 22 07 21222-21232 |
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10.1007/s11356-017-9671-4 doi (DE-627)OLC2040497617 (DE-He213)s11356-017-9671-4-p DE-627 ger DE-627 rakwb eng 570 360 333.7 VZ 690 333.7 540 VZ BIODIV DE-30 fid Dhanabalan, Vignaesh verfasserin aut Effect of processing conditions on degree of hydrolysis, ACE inhibition, and antioxidant activities of protein hydrolysate from Acetes indicus 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany 2017 Abstract Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using central composite design. The optimum conditions for enzyme-substrate ratio (mL/100 g) of 1.57, 1.69, 1.60, 1.56, and 1.50 and for hydrolysis time of 97.18, 96.5, 98.15 min, 102.48, and 88.44 min were established for attaining maximum yield, degree of hydrolysis, 2,2-diphenyl-1-picrylhydrazyl, angiotensin I-converting enzyme-inhibiting activity, and metal-chelating activity, respectively. ABTS radical scavenging activity and reducing power assay of optimized protein hydrolysate were found to be increased with the increase in concentration. The higher value of 7.04 (μM Trolox/g), 87.95, and 77.24%, respectively for DPPH, ACE, and metal-chelating activity indicated that the A. indicus protein hydrolysates have beneficial biological properties that could be well-utilized in the application of functional foods and nutraceuticals. Graphical abstractᅟ Angiotensin I-converting enzyme Response surface methodology Degree of hydrolysis Reducing activity Xavier, Martin (orcid)0000-0001-5879-4016 aut Kannuchamy, Nagalakshmi aut Asha, Kurukkan Kunnath aut Singh, Chongtham Baru aut Balange, Amjad aut Enthalten in Environmental science and pollution research Springer Berlin Heidelberg, 1994 24(2017), 26 vom: 22. Juli, Seite 21222-21232 (DE-627)171335805 (DE-600)1178791-0 (DE-576)038875101 0944-1344 nnns volume:24 year:2017 number:26 day:22 month:07 pages:21222-21232 https://doi.org/10.1007/s11356-017-9671-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-UMW SSG-OLC-ARC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-FOR SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4219 GBV_ILN_4277 AR 24 2017 26 22 07 21222-21232 |
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10.1007/s11356-017-9671-4 doi (DE-627)OLC2040497617 (DE-He213)s11356-017-9671-4-p DE-627 ger DE-627 rakwb eng 570 360 333.7 VZ 690 333.7 540 VZ BIODIV DE-30 fid Dhanabalan, Vignaesh verfasserin aut Effect of processing conditions on degree of hydrolysis, ACE inhibition, and antioxidant activities of protein hydrolysate from Acetes indicus 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany 2017 Abstract Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using central composite design. The optimum conditions for enzyme-substrate ratio (mL/100 g) of 1.57, 1.69, 1.60, 1.56, and 1.50 and for hydrolysis time of 97.18, 96.5, 98.15 min, 102.48, and 88.44 min were established for attaining maximum yield, degree of hydrolysis, 2,2-diphenyl-1-picrylhydrazyl, angiotensin I-converting enzyme-inhibiting activity, and metal-chelating activity, respectively. ABTS radical scavenging activity and reducing power assay of optimized protein hydrolysate were found to be increased with the increase in concentration. The higher value of 7.04 (μM Trolox/g), 87.95, and 77.24%, respectively for DPPH, ACE, and metal-chelating activity indicated that the A. indicus protein hydrolysates have beneficial biological properties that could be well-utilized in the application of functional foods and nutraceuticals. Graphical abstractᅟ Angiotensin I-converting enzyme Response surface methodology Degree of hydrolysis Reducing activity Xavier, Martin (orcid)0000-0001-5879-4016 aut Kannuchamy, Nagalakshmi aut Asha, Kurukkan Kunnath aut Singh, Chongtham Baru aut Balange, Amjad aut Enthalten in Environmental science and pollution research Springer Berlin Heidelberg, 1994 24(2017), 26 vom: 22. Juli, Seite 21222-21232 (DE-627)171335805 (DE-600)1178791-0 (DE-576)038875101 0944-1344 nnns volume:24 year:2017 number:26 day:22 month:07 pages:21222-21232 https://doi.org/10.1007/s11356-017-9671-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-UMW SSG-OLC-ARC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-FOR SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4219 GBV_ILN_4277 AR 24 2017 26 22 07 21222-21232 |
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10.1007/s11356-017-9671-4 doi (DE-627)OLC2040497617 (DE-He213)s11356-017-9671-4-p DE-627 ger DE-627 rakwb eng 570 360 333.7 VZ 690 333.7 540 VZ BIODIV DE-30 fid Dhanabalan, Vignaesh verfasserin aut Effect of processing conditions on degree of hydrolysis, ACE inhibition, and antioxidant activities of protein hydrolysate from Acetes indicus 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany 2017 Abstract Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using central composite design. The optimum conditions for enzyme-substrate ratio (mL/100 g) of 1.57, 1.69, 1.60, 1.56, and 1.50 and for hydrolysis time of 97.18, 96.5, 98.15 min, 102.48, and 88.44 min were established for attaining maximum yield, degree of hydrolysis, 2,2-diphenyl-1-picrylhydrazyl, angiotensin I-converting enzyme-inhibiting activity, and metal-chelating activity, respectively. ABTS radical scavenging activity and reducing power assay of optimized protein hydrolysate were found to be increased with the increase in concentration. The higher value of 7.04 (μM Trolox/g), 87.95, and 77.24%, respectively for DPPH, ACE, and metal-chelating activity indicated that the A. indicus protein hydrolysates have beneficial biological properties that could be well-utilized in the application of functional foods and nutraceuticals. Graphical abstractᅟ Angiotensin I-converting enzyme Response surface methodology Degree of hydrolysis Reducing activity Xavier, Martin (orcid)0000-0001-5879-4016 aut Kannuchamy, Nagalakshmi aut Asha, Kurukkan Kunnath aut Singh, Chongtham Baru aut Balange, Amjad aut Enthalten in Environmental science and pollution research Springer Berlin Heidelberg, 1994 24(2017), 26 vom: 22. Juli, Seite 21222-21232 (DE-627)171335805 (DE-600)1178791-0 (DE-576)038875101 0944-1344 nnns volume:24 year:2017 number:26 day:22 month:07 pages:21222-21232 https://doi.org/10.1007/s11356-017-9671-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-UMW SSG-OLC-ARC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-FOR SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4219 GBV_ILN_4277 AR 24 2017 26 22 07 21222-21232 |
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10.1007/s11356-017-9671-4 doi (DE-627)OLC2040497617 (DE-He213)s11356-017-9671-4-p DE-627 ger DE-627 rakwb eng 570 360 333.7 VZ 690 333.7 540 VZ BIODIV DE-30 fid Dhanabalan, Vignaesh verfasserin aut Effect of processing conditions on degree of hydrolysis, ACE inhibition, and antioxidant activities of protein hydrolysate from Acetes indicus 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag GmbH Germany 2017 Abstract Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using central composite design. The optimum conditions for enzyme-substrate ratio (mL/100 g) of 1.57, 1.69, 1.60, 1.56, and 1.50 and for hydrolysis time of 97.18, 96.5, 98.15 min, 102.48, and 88.44 min were established for attaining maximum yield, degree of hydrolysis, 2,2-diphenyl-1-picrylhydrazyl, angiotensin I-converting enzyme-inhibiting activity, and metal-chelating activity, respectively. ABTS radical scavenging activity and reducing power assay of optimized protein hydrolysate were found to be increased with the increase in concentration. The higher value of 7.04 (μM Trolox/g), 87.95, and 77.24%, respectively for DPPH, ACE, and metal-chelating activity indicated that the A. indicus protein hydrolysates have beneficial biological properties that could be well-utilized in the application of functional foods and nutraceuticals. Graphical abstractᅟ Angiotensin I-converting enzyme Response surface methodology Degree of hydrolysis Reducing activity Xavier, Martin (orcid)0000-0001-5879-4016 aut Kannuchamy, Nagalakshmi aut Asha, Kurukkan Kunnath aut Singh, Chongtham Baru aut Balange, Amjad aut Enthalten in Environmental science and pollution research Springer Berlin Heidelberg, 1994 24(2017), 26 vom: 22. Juli, Seite 21222-21232 (DE-627)171335805 (DE-600)1178791-0 (DE-576)038875101 0944-1344 nnns volume:24 year:2017 number:26 day:22 month:07 pages:21222-21232 https://doi.org/10.1007/s11356-017-9671-4 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-UMW SSG-OLC-ARC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-FOR SSG-OLC-DE-84 GBV_ILN_70 GBV_ILN_252 GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4219 GBV_ILN_4277 AR 24 2017 26 22 07 21222-21232 |
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Enthalten in Environmental science and pollution research 24(2017), 26 vom: 22. Juli, Seite 21222-21232 volume:24 year:2017 number:26 day:22 month:07 pages:21222-21232 |
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Effect of processing conditions on degree of hydrolysis, ACE inhibition, and antioxidant activities of protein hydrolysate from Acetes indicus |
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effect of processing conditions on degree of hydrolysis, ace inhibition, and antioxidant activities of protein hydrolysate from acetes indicus |
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Effect of processing conditions on degree of hydrolysis, ACE inhibition, and antioxidant activities of protein hydrolysate from Acetes indicus |
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Abstract Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using central composite design. The optimum conditions for enzyme-substrate ratio (mL/100 g) of 1.57, 1.69, 1.60, 1.56, and 1.50 and for hydrolysis time of 97.18, 96.5, 98.15 min, 102.48, and 88.44 min were established for attaining maximum yield, degree of hydrolysis, 2,2-diphenyl-1-picrylhydrazyl, angiotensin I-converting enzyme-inhibiting activity, and metal-chelating activity, respectively. ABTS radical scavenging activity and reducing power assay of optimized protein hydrolysate were found to be increased with the increase in concentration. The higher value of 7.04 (μM Trolox/g), 87.95, and 77.24%, respectively for DPPH, ACE, and metal-chelating activity indicated that the A. indicus protein hydrolysates have beneficial biological properties that could be well-utilized in the application of functional foods and nutraceuticals. Graphical abstractᅟ © Springer-Verlag GmbH Germany 2017 |
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Abstract Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using central composite design. The optimum conditions for enzyme-substrate ratio (mL/100 g) of 1.57, 1.69, 1.60, 1.56, and 1.50 and for hydrolysis time of 97.18, 96.5, 98.15 min, 102.48, and 88.44 min were established for attaining maximum yield, degree of hydrolysis, 2,2-diphenyl-1-picrylhydrazyl, angiotensin I-converting enzyme-inhibiting activity, and metal-chelating activity, respectively. ABTS radical scavenging activity and reducing power assay of optimized protein hydrolysate were found to be increased with the increase in concentration. The higher value of 7.04 (μM Trolox/g), 87.95, and 77.24%, respectively for DPPH, ACE, and metal-chelating activity indicated that the A. indicus protein hydrolysates have beneficial biological properties that could be well-utilized in the application of functional foods and nutraceuticals. Graphical abstractᅟ © Springer-Verlag GmbH Germany 2017 |
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Abstract Protein hydrolysate was prepared from Acetes indicus which is a major bycatch among non-penaeid prawn landings of India. Hydrolysis conditions (enzyme to substrate ratio and time) for preparing protein hydrolysates using alcalase enzyme were optimized by response surface methodology using central composite design. The optimum conditions for enzyme-substrate ratio (mL/100 g) of 1.57, 1.69, 1.60, 1.56, and 1.50 and for hydrolysis time of 97.18, 96.5, 98.15 min, 102.48, and 88.44 min were established for attaining maximum yield, degree of hydrolysis, 2,2-diphenyl-1-picrylhydrazyl, angiotensin I-converting enzyme-inhibiting activity, and metal-chelating activity, respectively. ABTS radical scavenging activity and reducing power assay of optimized protein hydrolysate were found to be increased with the increase in concentration. The higher value of 7.04 (μM Trolox/g), 87.95, and 77.24%, respectively for DPPH, ACE, and metal-chelating activity indicated that the A. indicus protein hydrolysates have beneficial biological properties that could be well-utilized in the application of functional foods and nutraceuticals. Graphical abstractᅟ © Springer-Verlag GmbH Germany 2017 |
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