Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity
Abstract A protease from Withania coagulans fruits was evaluated for milk-clotting properties. The optimum temperature and pH for enzyme activity were 70°C and 4, respectively. The protease also exhibited an excellent thermal stability at 60°C for 30 min. Fractional precipitation using ammonium sulf...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Beigomi, Maryam [verfasserIn] Mohammadifar, Mohammad Amin [verfasserIn] Hashemi, Maryam [verfasserIn] rohani, Mohsen Ghods [verfasserIn] Senthil, Kalaiselvi [verfasserIn] Valizadeh, Mohharam [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2014 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Food science and biotechnology - Sŏul : Korean Society of Food Science and Technology, 2010, 23(2014), 6 vom: Dez., Seite 1805-1813 |
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| Übergeordnetes Werk: |
volume:23 ; year:2014 ; number:6 ; month:12 ; pages:1805-1813 |
| Links: |
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| DOI / URN: |
10.1007/s10068-014-0247-5 |
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| Katalog-ID: |
SPR008550026 |
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| 024 | 7 | |a 10.1007/s10068-014-0247-5 |2 doi | |
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| 082 | 0 | 4 | |a 630 |a 640 |a 570 |q ASE |
| 100 | 1 | |a Beigomi, Maryam |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity |
| 264 | 1 | |c 2014 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
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| 520 | |a Abstract A protease from Withania coagulans fruits was evaluated for milk-clotting properties. The optimum temperature and pH for enzyme activity were 70°C and 4, respectively. The protease also exhibited an excellent thermal stability at 60°C for 30 min. Fractional precipitation using ammonium sulfate showed that the 40–50% fraction (F5) possessed the highest milk-clotting activity. The F5 fraction showed a Mw band of 66 kDa by SDS-PAGE. Gel formation was monitored using low amplitude oscillatory rheology at different temperatures. An Arrhenius plot was used to describe the temperature dependence of the gelation rate parameter. Time sweep testing showed that an increase in temperature was accompanied by a decrease in the gelation onset time, a higher gel formation rate, and higher values for final gel strength. W.coagulans fruits have potential for use as a rennet substitute. | ||
| 650 | 4 | |a rheology |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a milk-clotting |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a extraction |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a molecular weight |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Mohammadifar, Mohammad Amin |e verfasserin |4 aut | |
| 700 | 1 | |a Hashemi, Maryam |e verfasserin |4 aut | |
| 700 | 1 | |a rohani, Mohsen Ghods |e verfasserin |4 aut | |
| 700 | 1 | |a Senthil, Kalaiselvi |e verfasserin |4 aut | |
| 700 | 1 | |a Valizadeh, Mohharam |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Food science and biotechnology |d Sŏul : Korean Society of Food Science and Technology, 2010 |g 23(2014), 6 vom: Dez., Seite 1805-1813 |w (DE-627)624822982 |w (DE-600)2549899-X |x 2092-6456 |7 nnns |
| 773 | 1 | 8 | |g volume:23 |g year:2014 |g number:6 |g month:12 |g pages:1805-1813 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1007/s10068-014-0247-5 |z lizenzpflichtig |3 Volltext |
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| 912 | |a SYSFLAG_A | ||
| 912 | |a GBV_SPRINGER | ||
| 912 | |a SSG-OLC-PHA | ||
| 912 | |a GBV_ILN_11 | ||
| 912 | |a GBV_ILN_20 | ||
| 912 | |a GBV_ILN_22 | ||
| 912 | |a GBV_ILN_23 | ||
| 912 | |a GBV_ILN_24 | ||
| 912 | |a GBV_ILN_31 | ||
| 912 | |a GBV_ILN_32 | ||
| 912 | |a GBV_ILN_39 | ||
| 912 | |a GBV_ILN_40 | ||
| 912 | |a GBV_ILN_60 | ||
| 912 | |a GBV_ILN_62 | ||
| 912 | |a GBV_ILN_63 | ||
| 912 | |a GBV_ILN_65 | ||
| 912 | |a GBV_ILN_69 | ||
| 912 | |a GBV_ILN_70 | ||
| 912 | |a GBV_ILN_73 | ||
| 912 | |a GBV_ILN_74 | ||
| 912 | |a GBV_ILN_90 | ||
| 912 | |a GBV_ILN_95 | ||
| 912 | |a GBV_ILN_100 | ||
| 912 | |a GBV_ILN_101 | ||
| 912 | |a GBV_ILN_105 | ||
| 912 | |a GBV_ILN_110 | ||
| 912 | |a GBV_ILN_120 | ||
| 912 | |a GBV_ILN_138 | ||
| 912 | |a GBV_ILN_150 | ||
| 912 | |a GBV_ILN_151 | ||
| 912 | |a GBV_ILN_152 | ||
| 912 | |a GBV_ILN_161 | ||
| 912 | |a GBV_ILN_170 | ||
| 912 | |a GBV_ILN_171 | ||
| 912 | |a GBV_ILN_187 | ||
| 912 | |a GBV_ILN_213 | ||
| 912 | |a GBV_ILN_224 | ||
| 912 | |a GBV_ILN_230 | ||
| 912 | |a GBV_ILN_250 | ||
| 912 | |a GBV_ILN_281 | ||
| 912 | |a GBV_ILN_285 | ||
| 912 | |a GBV_ILN_293 | ||
| 912 | |a GBV_ILN_370 | ||
| 912 | |a GBV_ILN_602 | ||
| 912 | |a GBV_ILN_636 | ||
| 912 | |a GBV_ILN_702 | ||
| 912 | |a GBV_ILN_2001 | ||
| 912 | |a GBV_ILN_2003 | ||
| 912 | |a GBV_ILN_2004 | ||
| 912 | |a GBV_ILN_2005 | ||
| 912 | |a GBV_ILN_2006 | ||
| 912 | |a GBV_ILN_2007 | ||
| 912 | |a GBV_ILN_2008 | ||
| 912 | |a GBV_ILN_2009 | ||
| 912 | |a GBV_ILN_2010 | ||
| 912 | |a GBV_ILN_2011 | ||
| 912 | |a GBV_ILN_2014 | ||
| 912 | |a GBV_ILN_2015 | ||
| 912 | |a GBV_ILN_2020 | ||
| 912 | |a GBV_ILN_2021 | ||
| 912 | |a GBV_ILN_2025 | ||
| 912 | |a GBV_ILN_2026 | ||
| 912 | |a GBV_ILN_2027 | ||
| 912 | |a GBV_ILN_2031 | ||
| 912 | |a GBV_ILN_2034 | ||
| 912 | |a GBV_ILN_2037 | ||
| 912 | |a GBV_ILN_2038 | ||
| 912 | |a GBV_ILN_2039 | ||
| 912 | |a GBV_ILN_2044 | ||
| 912 | |a GBV_ILN_2048 | ||
| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2055 | ||
| 912 | |a GBV_ILN_2057 | ||
| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2065 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2070 | ||
| 912 | |a GBV_ILN_2086 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2093 | ||
| 912 | |a GBV_ILN_2106 | ||
| 912 | |a GBV_ILN_2107 | ||
| 912 | |a GBV_ILN_2108 | ||
| 912 | |a GBV_ILN_2110 | ||
| 912 | |a GBV_ILN_2111 | ||
| 912 | |a GBV_ILN_2112 | ||
| 912 | |a GBV_ILN_2113 | ||
| 912 | |a GBV_ILN_2116 | ||
| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2119 | ||
| 912 | |a GBV_ILN_2122 | ||
| 912 | |a GBV_ILN_2129 | ||
| 912 | |a GBV_ILN_2143 | ||
| 912 | |a GBV_ILN_2144 | ||
| 912 | |a GBV_ILN_2147 | ||
| 912 | |a GBV_ILN_2148 | ||
| 912 | |a GBV_ILN_2152 | ||
| 912 | |a GBV_ILN_2153 | ||
| 912 | |a GBV_ILN_2188 | ||
| 912 | |a GBV_ILN_2190 | ||
| 912 | |a GBV_ILN_2232 | ||
| 912 | |a GBV_ILN_2336 | ||
| 912 | |a GBV_ILN_2446 | ||
| 912 | |a GBV_ILN_2470 | ||
| 912 | |a GBV_ILN_2472 | ||
| 912 | |a GBV_ILN_2507 | ||
| 912 | |a GBV_ILN_2522 | ||
| 912 | |a GBV_ILN_2548 | ||
| 912 | |a GBV_ILN_4035 | ||
| 912 | |a GBV_ILN_4037 | ||
| 912 | |a GBV_ILN_4046 | ||
| 912 | |a GBV_ILN_4112 | ||
| 912 | |a GBV_ILN_4125 | ||
| 912 | |a GBV_ILN_4242 | ||
| 912 | |a GBV_ILN_4246 | ||
| 912 | |a GBV_ILN_4249 | ||
| 912 | |a GBV_ILN_4251 | ||
| 912 | |a GBV_ILN_4305 | ||
| 912 | |a GBV_ILN_4306 | ||
| 912 | |a GBV_ILN_4307 | ||
| 912 | |a GBV_ILN_4313 | ||
| 912 | |a GBV_ILN_4322 | ||
| 912 | |a GBV_ILN_4323 | ||
| 912 | |a GBV_ILN_4324 | ||
| 912 | |a GBV_ILN_4325 | ||
| 912 | |a GBV_ILN_4326 | ||
| 912 | |a GBV_ILN_4333 | ||
| 912 | |a GBV_ILN_4334 | ||
| 912 | |a GBV_ILN_4335 | ||
| 912 | |a GBV_ILN_4336 | ||
| 912 | |a GBV_ILN_4338 | ||
| 912 | |a GBV_ILN_4393 | ||
| 912 | |a GBV_ILN_4700 | ||
| 951 | |a AR | ||
| 952 | |d 23 |j 2014 |e 6 |c 12 |h 1805-1813 | ||
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2014 |
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10.1007/s10068-014-0247-5 doi (DE-627)SPR008550026 (SPR)s10068-014-0247-5-e DE-627 ger DE-627 rakwb eng 630 640 570 ASE Beigomi, Maryam verfasserin aut Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A protease from Withania coagulans fruits was evaluated for milk-clotting properties. The optimum temperature and pH for enzyme activity were 70°C and 4, respectively. The protease also exhibited an excellent thermal stability at 60°C for 30 min. Fractional precipitation using ammonium sulfate showed that the 40–50% fraction (F5) possessed the highest milk-clotting activity. The F5 fraction showed a Mw band of 66 kDa by SDS-PAGE. Gel formation was monitored using low amplitude oscillatory rheology at different temperatures. An Arrhenius plot was used to describe the temperature dependence of the gelation rate parameter. Time sweep testing showed that an increase in temperature was accompanied by a decrease in the gelation onset time, a higher gel formation rate, and higher values for final gel strength. W.coagulans fruits have potential for use as a rennet substitute. rheology (dpeaa)DE-He213 milk-clotting (dpeaa)DE-He213 extraction (dpeaa)DE-He213 molecular weight (dpeaa)DE-He213 Mohammadifar, Mohammad Amin verfasserin aut Hashemi, Maryam verfasserin aut rohani, Mohsen Ghods verfasserin aut Senthil, Kalaiselvi verfasserin aut Valizadeh, Mohharam verfasserin aut Enthalten in Food science and biotechnology Sŏul : Korean Society of Food Science and Technology, 2010 23(2014), 6 vom: Dez., Seite 1805-1813 (DE-627)624822982 (DE-600)2549899-X 2092-6456 nnns volume:23 year:2014 number:6 month:12 pages:1805-1813 https://dx.doi.org/10.1007/s10068-014-0247-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 23 2014 6 12 1805-1813 |
| spelling |
10.1007/s10068-014-0247-5 doi (DE-627)SPR008550026 (SPR)s10068-014-0247-5-e DE-627 ger DE-627 rakwb eng 630 640 570 ASE Beigomi, Maryam verfasserin aut Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A protease from Withania coagulans fruits was evaluated for milk-clotting properties. The optimum temperature and pH for enzyme activity were 70°C and 4, respectively. The protease also exhibited an excellent thermal stability at 60°C for 30 min. Fractional precipitation using ammonium sulfate showed that the 40–50% fraction (F5) possessed the highest milk-clotting activity. The F5 fraction showed a Mw band of 66 kDa by SDS-PAGE. Gel formation was monitored using low amplitude oscillatory rheology at different temperatures. An Arrhenius plot was used to describe the temperature dependence of the gelation rate parameter. Time sweep testing showed that an increase in temperature was accompanied by a decrease in the gelation onset time, a higher gel formation rate, and higher values for final gel strength. W.coagulans fruits have potential for use as a rennet substitute. rheology (dpeaa)DE-He213 milk-clotting (dpeaa)DE-He213 extraction (dpeaa)DE-He213 molecular weight (dpeaa)DE-He213 Mohammadifar, Mohammad Amin verfasserin aut Hashemi, Maryam verfasserin aut rohani, Mohsen Ghods verfasserin aut Senthil, Kalaiselvi verfasserin aut Valizadeh, Mohharam verfasserin aut Enthalten in Food science and biotechnology Sŏul : Korean Society of Food Science and Technology, 2010 23(2014), 6 vom: Dez., Seite 1805-1813 (DE-627)624822982 (DE-600)2549899-X 2092-6456 nnns volume:23 year:2014 number:6 month:12 pages:1805-1813 https://dx.doi.org/10.1007/s10068-014-0247-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 23 2014 6 12 1805-1813 |
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10.1007/s10068-014-0247-5 doi (DE-627)SPR008550026 (SPR)s10068-014-0247-5-e DE-627 ger DE-627 rakwb eng 630 640 570 ASE Beigomi, Maryam verfasserin aut Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A protease from Withania coagulans fruits was evaluated for milk-clotting properties. The optimum temperature and pH for enzyme activity were 70°C and 4, respectively. The protease also exhibited an excellent thermal stability at 60°C for 30 min. Fractional precipitation using ammonium sulfate showed that the 40–50% fraction (F5) possessed the highest milk-clotting activity. The F5 fraction showed a Mw band of 66 kDa by SDS-PAGE. Gel formation was monitored using low amplitude oscillatory rheology at different temperatures. An Arrhenius plot was used to describe the temperature dependence of the gelation rate parameter. Time sweep testing showed that an increase in temperature was accompanied by a decrease in the gelation onset time, a higher gel formation rate, and higher values for final gel strength. W.coagulans fruits have potential for use as a rennet substitute. rheology (dpeaa)DE-He213 milk-clotting (dpeaa)DE-He213 extraction (dpeaa)DE-He213 molecular weight (dpeaa)DE-He213 Mohammadifar, Mohammad Amin verfasserin aut Hashemi, Maryam verfasserin aut rohani, Mohsen Ghods verfasserin aut Senthil, Kalaiselvi verfasserin aut Valizadeh, Mohharam verfasserin aut Enthalten in Food science and biotechnology Sŏul : Korean Society of Food Science and Technology, 2010 23(2014), 6 vom: Dez., Seite 1805-1813 (DE-627)624822982 (DE-600)2549899-X 2092-6456 nnns volume:23 year:2014 number:6 month:12 pages:1805-1813 https://dx.doi.org/10.1007/s10068-014-0247-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 23 2014 6 12 1805-1813 |
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10.1007/s10068-014-0247-5 doi (DE-627)SPR008550026 (SPR)s10068-014-0247-5-e DE-627 ger DE-627 rakwb eng 630 640 570 ASE Beigomi, Maryam verfasserin aut Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A protease from Withania coagulans fruits was evaluated for milk-clotting properties. The optimum temperature and pH for enzyme activity were 70°C and 4, respectively. The protease also exhibited an excellent thermal stability at 60°C for 30 min. Fractional precipitation using ammonium sulfate showed that the 40–50% fraction (F5) possessed the highest milk-clotting activity. The F5 fraction showed a Mw band of 66 kDa by SDS-PAGE. Gel formation was monitored using low amplitude oscillatory rheology at different temperatures. An Arrhenius plot was used to describe the temperature dependence of the gelation rate parameter. Time sweep testing showed that an increase in temperature was accompanied by a decrease in the gelation onset time, a higher gel formation rate, and higher values for final gel strength. W.coagulans fruits have potential for use as a rennet substitute. rheology (dpeaa)DE-He213 milk-clotting (dpeaa)DE-He213 extraction (dpeaa)DE-He213 molecular weight (dpeaa)DE-He213 Mohammadifar, Mohammad Amin verfasserin aut Hashemi, Maryam verfasserin aut rohani, Mohsen Ghods verfasserin aut Senthil, Kalaiselvi verfasserin aut Valizadeh, Mohharam verfasserin aut Enthalten in Food science and biotechnology Sŏul : Korean Society of Food Science and Technology, 2010 23(2014), 6 vom: Dez., Seite 1805-1813 (DE-627)624822982 (DE-600)2549899-X 2092-6456 nnns volume:23 year:2014 number:6 month:12 pages:1805-1813 https://dx.doi.org/10.1007/s10068-014-0247-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 23 2014 6 12 1805-1813 |
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10.1007/s10068-014-0247-5 doi (DE-627)SPR008550026 (SPR)s10068-014-0247-5-e DE-627 ger DE-627 rakwb eng 630 640 570 ASE Beigomi, Maryam verfasserin aut Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A protease from Withania coagulans fruits was evaluated for milk-clotting properties. The optimum temperature and pH for enzyme activity were 70°C and 4, respectively. The protease also exhibited an excellent thermal stability at 60°C for 30 min. Fractional precipitation using ammonium sulfate showed that the 40–50% fraction (F5) possessed the highest milk-clotting activity. The F5 fraction showed a Mw band of 66 kDa by SDS-PAGE. Gel formation was monitored using low amplitude oscillatory rheology at different temperatures. An Arrhenius plot was used to describe the temperature dependence of the gelation rate parameter. Time sweep testing showed that an increase in temperature was accompanied by a decrease in the gelation onset time, a higher gel formation rate, and higher values for final gel strength. W.coagulans fruits have potential for use as a rennet substitute. rheology (dpeaa)DE-He213 milk-clotting (dpeaa)DE-He213 extraction (dpeaa)DE-He213 molecular weight (dpeaa)DE-He213 Mohammadifar, Mohammad Amin verfasserin aut Hashemi, Maryam verfasserin aut rohani, Mohsen Ghods verfasserin aut Senthil, Kalaiselvi verfasserin aut Valizadeh, Mohharam verfasserin aut Enthalten in Food science and biotechnology Sŏul : Korean Society of Food Science and Technology, 2010 23(2014), 6 vom: Dez., Seite 1805-1813 (DE-627)624822982 (DE-600)2549899-X 2092-6456 nnns volume:23 year:2014 number:6 month:12 pages:1805-1813 https://dx.doi.org/10.1007/s10068-014-0247-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 23 2014 6 12 1805-1813 |
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English |
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Enthalten in Food science and biotechnology 23(2014), 6 vom: Dez., Seite 1805-1813 volume:23 year:2014 number:6 month:12 pages:1805-1813 |
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Enthalten in Food science and biotechnology 23(2014), 6 vom: Dez., Seite 1805-1813 volume:23 year:2014 number:6 month:12 pages:1805-1813 |
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Food science and biotechnology |
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Beigomi, Maryam @@aut@@ Mohammadifar, Mohammad Amin @@aut@@ Hashemi, Maryam @@aut@@ rohani, Mohsen Ghods @@aut@@ Senthil, Kalaiselvi @@aut@@ Valizadeh, Mohharam @@aut@@ |
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2014-12-01T00:00:00Z |
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Beigomi, Maryam |
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630 640 570 ASE Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity rheology (dpeaa)DE-He213 milk-clotting (dpeaa)DE-He213 extraction (dpeaa)DE-He213 molecular weight (dpeaa)DE-He213 |
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Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity |
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Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity |
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Beigomi, Maryam |
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Food science and biotechnology |
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biochemical and rheological characterization of a protease from fruits of withania coagulans with a milk-clotting activity |
| title_auth |
Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity |
| abstract |
Abstract A protease from Withania coagulans fruits was evaluated for milk-clotting properties. The optimum temperature and pH for enzyme activity were 70°C and 4, respectively. The protease also exhibited an excellent thermal stability at 60°C for 30 min. Fractional precipitation using ammonium sulfate showed that the 40–50% fraction (F5) possessed the highest milk-clotting activity. The F5 fraction showed a Mw band of 66 kDa by SDS-PAGE. Gel formation was monitored using low amplitude oscillatory rheology at different temperatures. An Arrhenius plot was used to describe the temperature dependence of the gelation rate parameter. Time sweep testing showed that an increase in temperature was accompanied by a decrease in the gelation onset time, a higher gel formation rate, and higher values for final gel strength. W.coagulans fruits have potential for use as a rennet substitute. |
| abstractGer |
Abstract A protease from Withania coagulans fruits was evaluated for milk-clotting properties. The optimum temperature and pH for enzyme activity were 70°C and 4, respectively. The protease also exhibited an excellent thermal stability at 60°C for 30 min. Fractional precipitation using ammonium sulfate showed that the 40–50% fraction (F5) possessed the highest milk-clotting activity. The F5 fraction showed a Mw band of 66 kDa by SDS-PAGE. Gel formation was monitored using low amplitude oscillatory rheology at different temperatures. An Arrhenius plot was used to describe the temperature dependence of the gelation rate parameter. Time sweep testing showed that an increase in temperature was accompanied by a decrease in the gelation onset time, a higher gel formation rate, and higher values for final gel strength. W.coagulans fruits have potential for use as a rennet substitute. |
| abstract_unstemmed |
Abstract A protease from Withania coagulans fruits was evaluated for milk-clotting properties. The optimum temperature and pH for enzyme activity were 70°C and 4, respectively. The protease also exhibited an excellent thermal stability at 60°C for 30 min. Fractional precipitation using ammonium sulfate showed that the 40–50% fraction (F5) possessed the highest milk-clotting activity. The F5 fraction showed a Mw band of 66 kDa by SDS-PAGE. Gel formation was monitored using low amplitude oscillatory rheology at different temperatures. An Arrhenius plot was used to describe the temperature dependence of the gelation rate parameter. Time sweep testing showed that an increase in temperature was accompanied by a decrease in the gelation onset time, a higher gel formation rate, and higher values for final gel strength. W.coagulans fruits have potential for use as a rennet substitute. |
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6 |
| title_short |
Biochemical and rheological characterization of a protease from fruits of Withania coagulans with a milk-clotting activity |
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https://dx.doi.org/10.1007/s10068-014-0247-5 |
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Mohammadifar, Mohammad Amin Hashemi, Maryam rohani, Mohsen Ghods Senthil, Kalaiselvi Valizadeh, Mohharam |
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Mohammadifar, Mohammad Amin Hashemi, Maryam rohani, Mohsen Ghods Senthil, Kalaiselvi Valizadeh, Mohharam |
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| doi_str |
10.1007/s10068-014-0247-5 |
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2024-07-03T21:46:50.827Z |
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| score |
7.399658 |