Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein
Abstract The steady increase in world cheese demand keeps the search for appropriate coagulating enzymes as rennet substitutes in the scientific focus. This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate...
Ausführliche Beschreibung
Autor*in: |
Anusha, R. [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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Anmerkung: |
© Springer-Verlag Berlin Heidelberg 2014 |
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Übergeordnetes Werk: |
Enthalten in: European food research and technology - Berlin : Springer, 1999, 238(2014), 6 vom: 18. Feb., Seite 997-1006 |
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Übergeordnetes Werk: |
volume:238 ; year:2014 ; number:6 ; day:18 ; month:02 ; pages:997-1006 |
Links: |
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DOI / URN: |
10.1007/s00217-014-2177-0 |
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Katalog-ID: |
SPR002309440 |
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245 | 1 | 0 | |a Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein |
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520 | |a Abstract The steady increase in world cheese demand keeps the search for appropriate coagulating enzymes as rennet substitutes in the scientific focus. This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate. CE from latex exhibited high caseinolytic (86.445 ± 1.055 U/ml) as well as milk-clotting activity (450 U/ml) when compared to other parts. Significant milk clotting index (MCI) was presented by crude enzyme of latex followed by stem, flower and leaf in the decreasing order (p < 0.05). CE from all parts showed an optimum activity at 37 °C, pH 5.5 and 10 mM calcium chloride concentration with excellent pH (4.5–6.5) and thermal stability (30–60 °C). Hydrolysis pattern of casein components by CE during 1 h incubation, as assessed by Tricine–SDS-PAGE, and subsequent peak analysis revealed CE from stem to be closely similar to that of rennin. However, extensive casein hydrolysis was observed when incubated with crude latex enzyme. Casein bands of CE and rennin tended to disappear as incubation progressed to 24 h. Proteolytic degradation was found to be advanced and resulted in complete breakdown of casein fractions unravelling the importance of incubation time as a possible essential requisite for controlled and appropriate casein hydrolysis. The study provides evidence of rennin-like activity associated with C. gigantea plant parts which may serve as a promising source of vegetable milk coagulant. | ||
650 | 4 | |a Milk clotting |7 (dpeaa)DE-He213 | |
650 | 4 | |a Proteases |7 (dpeaa)DE-He213 | |
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700 | 1 | |a Singh, Maheshwari Kumari |4 aut | |
700 | 1 | |a Bindhu, O. S. |4 aut | |
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2014 |
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10.1007/s00217-014-2177-0 doi (DE-627)SPR002309440 (SPR)s00217-014-2177-0-e DE-627 ger DE-627 rakwb eng Anusha, R. verfasserin aut Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag Berlin Heidelberg 2014 Abstract The steady increase in world cheese demand keeps the search for appropriate coagulating enzymes as rennet substitutes in the scientific focus. This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate. CE from latex exhibited high caseinolytic (86.445 ± 1.055 U/ml) as well as milk-clotting activity (450 U/ml) when compared to other parts. Significant milk clotting index (MCI) was presented by crude enzyme of latex followed by stem, flower and leaf in the decreasing order (p < 0.05). CE from all parts showed an optimum activity at 37 °C, pH 5.5 and 10 mM calcium chloride concentration with excellent pH (4.5–6.5) and thermal stability (30–60 °C). Hydrolysis pattern of casein components by CE during 1 h incubation, as assessed by Tricine–SDS-PAGE, and subsequent peak analysis revealed CE from stem to be closely similar to that of rennin. However, extensive casein hydrolysis was observed when incubated with crude latex enzyme. Casein bands of CE and rennin tended to disappear as incubation progressed to 24 h. Proteolytic degradation was found to be advanced and resulted in complete breakdown of casein fractions unravelling the importance of incubation time as a possible essential requisite for controlled and appropriate casein hydrolysis. The study provides evidence of rennin-like activity associated with C. gigantea plant parts which may serve as a promising source of vegetable milk coagulant. Milk clotting (dpeaa)DE-He213 Proteases (dpeaa)DE-He213 Vegetable coagulant (dpeaa)DE-He213 Singh, Maheshwari Kumari aut Bindhu, O. S. aut Enthalten in European food research and technology Berlin : Springer, 1999 238(2014), 6 vom: 18. Feb., Seite 997-1006 (DE-627)27012859X (DE-600)1476605-X 1438-2385 nnns volume:238 year:2014 number:6 day:18 month:02 pages:997-1006 https://dx.doi.org/10.1007/s00217-014-2177-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER 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_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 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_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 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 238 2014 6 18 02 997-1006 |
spelling |
10.1007/s00217-014-2177-0 doi (DE-627)SPR002309440 (SPR)s00217-014-2177-0-e DE-627 ger DE-627 rakwb eng Anusha, R. verfasserin aut Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag Berlin Heidelberg 2014 Abstract The steady increase in world cheese demand keeps the search for appropriate coagulating enzymes as rennet substitutes in the scientific focus. This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate. CE from latex exhibited high caseinolytic (86.445 ± 1.055 U/ml) as well as milk-clotting activity (450 U/ml) when compared to other parts. Significant milk clotting index (MCI) was presented by crude enzyme of latex followed by stem, flower and leaf in the decreasing order (p < 0.05). CE from all parts showed an optimum activity at 37 °C, pH 5.5 and 10 mM calcium chloride concentration with excellent pH (4.5–6.5) and thermal stability (30–60 °C). Hydrolysis pattern of casein components by CE during 1 h incubation, as assessed by Tricine–SDS-PAGE, and subsequent peak analysis revealed CE from stem to be closely similar to that of rennin. However, extensive casein hydrolysis was observed when incubated with crude latex enzyme. Casein bands of CE and rennin tended to disappear as incubation progressed to 24 h. Proteolytic degradation was found to be advanced and resulted in complete breakdown of casein fractions unravelling the importance of incubation time as a possible essential requisite for controlled and appropriate casein hydrolysis. The study provides evidence of rennin-like activity associated with C. gigantea plant parts which may serve as a promising source of vegetable milk coagulant. Milk clotting (dpeaa)DE-He213 Proteases (dpeaa)DE-He213 Vegetable coagulant (dpeaa)DE-He213 Singh, Maheshwari Kumari aut Bindhu, O. S. aut Enthalten in European food research and technology Berlin : Springer, 1999 238(2014), 6 vom: 18. Feb., Seite 997-1006 (DE-627)27012859X (DE-600)1476605-X 1438-2385 nnns volume:238 year:2014 number:6 day:18 month:02 pages:997-1006 https://dx.doi.org/10.1007/s00217-014-2177-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER 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_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 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_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 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 238 2014 6 18 02 997-1006 |
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10.1007/s00217-014-2177-0 doi (DE-627)SPR002309440 (SPR)s00217-014-2177-0-e DE-627 ger DE-627 rakwb eng Anusha, R. verfasserin aut Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag Berlin Heidelberg 2014 Abstract The steady increase in world cheese demand keeps the search for appropriate coagulating enzymes as rennet substitutes in the scientific focus. This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate. CE from latex exhibited high caseinolytic (86.445 ± 1.055 U/ml) as well as milk-clotting activity (450 U/ml) when compared to other parts. Significant milk clotting index (MCI) was presented by crude enzyme of latex followed by stem, flower and leaf in the decreasing order (p < 0.05). CE from all parts showed an optimum activity at 37 °C, pH 5.5 and 10 mM calcium chloride concentration with excellent pH (4.5–6.5) and thermal stability (30–60 °C). Hydrolysis pattern of casein components by CE during 1 h incubation, as assessed by Tricine–SDS-PAGE, and subsequent peak analysis revealed CE from stem to be closely similar to that of rennin. However, extensive casein hydrolysis was observed when incubated with crude latex enzyme. Casein bands of CE and rennin tended to disappear as incubation progressed to 24 h. Proteolytic degradation was found to be advanced and resulted in complete breakdown of casein fractions unravelling the importance of incubation time as a possible essential requisite for controlled and appropriate casein hydrolysis. The study provides evidence of rennin-like activity associated with C. gigantea plant parts which may serve as a promising source of vegetable milk coagulant. Milk clotting (dpeaa)DE-He213 Proteases (dpeaa)DE-He213 Vegetable coagulant (dpeaa)DE-He213 Singh, Maheshwari Kumari aut Bindhu, O. S. aut Enthalten in European food research and technology Berlin : Springer, 1999 238(2014), 6 vom: 18. Feb., Seite 997-1006 (DE-627)27012859X (DE-600)1476605-X 1438-2385 nnns volume:238 year:2014 number:6 day:18 month:02 pages:997-1006 https://dx.doi.org/10.1007/s00217-014-2177-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER 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_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 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_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 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 238 2014 6 18 02 997-1006 |
allfieldsGer |
10.1007/s00217-014-2177-0 doi (DE-627)SPR002309440 (SPR)s00217-014-2177-0-e DE-627 ger DE-627 rakwb eng Anusha, R. verfasserin aut Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag Berlin Heidelberg 2014 Abstract The steady increase in world cheese demand keeps the search for appropriate coagulating enzymes as rennet substitutes in the scientific focus. This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate. CE from latex exhibited high caseinolytic (86.445 ± 1.055 U/ml) as well as milk-clotting activity (450 U/ml) when compared to other parts. Significant milk clotting index (MCI) was presented by crude enzyme of latex followed by stem, flower and leaf in the decreasing order (p < 0.05). CE from all parts showed an optimum activity at 37 °C, pH 5.5 and 10 mM calcium chloride concentration with excellent pH (4.5–6.5) and thermal stability (30–60 °C). Hydrolysis pattern of casein components by CE during 1 h incubation, as assessed by Tricine–SDS-PAGE, and subsequent peak analysis revealed CE from stem to be closely similar to that of rennin. However, extensive casein hydrolysis was observed when incubated with crude latex enzyme. Casein bands of CE and rennin tended to disappear as incubation progressed to 24 h. Proteolytic degradation was found to be advanced and resulted in complete breakdown of casein fractions unravelling the importance of incubation time as a possible essential requisite for controlled and appropriate casein hydrolysis. The study provides evidence of rennin-like activity associated with C. gigantea plant parts which may serve as a promising source of vegetable milk coagulant. Milk clotting (dpeaa)DE-He213 Proteases (dpeaa)DE-He213 Vegetable coagulant (dpeaa)DE-He213 Singh, Maheshwari Kumari aut Bindhu, O. S. aut Enthalten in European food research and technology Berlin : Springer, 1999 238(2014), 6 vom: 18. Feb., Seite 997-1006 (DE-627)27012859X (DE-600)1476605-X 1438-2385 nnns volume:238 year:2014 number:6 day:18 month:02 pages:997-1006 https://dx.doi.org/10.1007/s00217-014-2177-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER 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_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 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_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 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 238 2014 6 18 02 997-1006 |
allfieldsSound |
10.1007/s00217-014-2177-0 doi (DE-627)SPR002309440 (SPR)s00217-014-2177-0-e DE-627 ger DE-627 rakwb eng Anusha, R. verfasserin aut Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag Berlin Heidelberg 2014 Abstract The steady increase in world cheese demand keeps the search for appropriate coagulating enzymes as rennet substitutes in the scientific focus. This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate. CE from latex exhibited high caseinolytic (86.445 ± 1.055 U/ml) as well as milk-clotting activity (450 U/ml) when compared to other parts. Significant milk clotting index (MCI) was presented by crude enzyme of latex followed by stem, flower and leaf in the decreasing order (p < 0.05). CE from all parts showed an optimum activity at 37 °C, pH 5.5 and 10 mM calcium chloride concentration with excellent pH (4.5–6.5) and thermal stability (30–60 °C). Hydrolysis pattern of casein components by CE during 1 h incubation, as assessed by Tricine–SDS-PAGE, and subsequent peak analysis revealed CE from stem to be closely similar to that of rennin. However, extensive casein hydrolysis was observed when incubated with crude latex enzyme. Casein bands of CE and rennin tended to disappear as incubation progressed to 24 h. Proteolytic degradation was found to be advanced and resulted in complete breakdown of casein fractions unravelling the importance of incubation time as a possible essential requisite for controlled and appropriate casein hydrolysis. The study provides evidence of rennin-like activity associated with C. gigantea plant parts which may serve as a promising source of vegetable milk coagulant. Milk clotting (dpeaa)DE-He213 Proteases (dpeaa)DE-He213 Vegetable coagulant (dpeaa)DE-He213 Singh, Maheshwari Kumari aut Bindhu, O. S. aut Enthalten in European food research and technology Berlin : Springer, 1999 238(2014), 6 vom: 18. Feb., Seite 997-1006 (DE-627)27012859X (DE-600)1476605-X 1438-2385 nnns volume:238 year:2014 number:6 day:18 month:02 pages:997-1006 https://dx.doi.org/10.1007/s00217-014-2177-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER 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_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 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_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 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 238 2014 6 18 02 997-1006 |
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Enthalten in European food research and technology 238(2014), 6 vom: 18. Feb., Seite 997-1006 volume:238 year:2014 number:6 day:18 month:02 pages:997-1006 |
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Enthalten in European food research and technology 238(2014), 6 vom: 18. Feb., Seite 997-1006 volume:238 year:2014 number:6 day:18 month:02 pages:997-1006 |
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Anusha, R. @@aut@@ Singh, Maheshwari Kumari @@aut@@ Bindhu, O. S. @@aut@@ |
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This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate. CE from latex exhibited high caseinolytic (86.445 ± 1.055 U/ml) as well as milk-clotting activity (450 U/ml) when compared to other parts. Significant milk clotting index (MCI) was presented by crude enzyme of latex followed by stem, flower and leaf in the decreasing order (p < 0.05). CE from all parts showed an optimum activity at 37 °C, pH 5.5 and 10 mM calcium chloride concentration with excellent pH (4.5–6.5) and thermal stability (30–60 °C). Hydrolysis pattern of casein components by CE during 1 h incubation, as assessed by Tricine–SDS-PAGE, and subsequent peak analysis revealed CE from stem to be closely similar to that of rennin. However, extensive casein hydrolysis was observed when incubated with crude latex enzyme. Casein bands of CE and rennin tended to disappear as incubation progressed to 24 h. Proteolytic degradation was found to be advanced and resulted in complete breakdown of casein fractions unravelling the importance of incubation time as a possible essential requisite for controlled and appropriate casein hydrolysis. 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Anusha, R. |
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Anusha, R. misc Milk clotting misc Proteases misc Vegetable coagulant Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein |
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Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein Milk clotting (dpeaa)DE-He213 Proteases (dpeaa)DE-He213 Vegetable coagulant (dpeaa)DE-He213 |
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Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein |
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Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein |
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Anusha, R. Singh, Maheshwari Kumari Bindhu, O. S. |
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characterisation of potential milk coagulants from calotropis gigantea plant parts and their hydrolytic pattern of bovine casein |
title_auth |
Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein |
abstract |
Abstract The steady increase in world cheese demand keeps the search for appropriate coagulating enzymes as rennet substitutes in the scientific focus. This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate. CE from latex exhibited high caseinolytic (86.445 ± 1.055 U/ml) as well as milk-clotting activity (450 U/ml) when compared to other parts. Significant milk clotting index (MCI) was presented by crude enzyme of latex followed by stem, flower and leaf in the decreasing order (p < 0.05). CE from all parts showed an optimum activity at 37 °C, pH 5.5 and 10 mM calcium chloride concentration with excellent pH (4.5–6.5) and thermal stability (30–60 °C). Hydrolysis pattern of casein components by CE during 1 h incubation, as assessed by Tricine–SDS-PAGE, and subsequent peak analysis revealed CE from stem to be closely similar to that of rennin. However, extensive casein hydrolysis was observed when incubated with crude latex enzyme. Casein bands of CE and rennin tended to disappear as incubation progressed to 24 h. Proteolytic degradation was found to be advanced and resulted in complete breakdown of casein fractions unravelling the importance of incubation time as a possible essential requisite for controlled and appropriate casein hydrolysis. The study provides evidence of rennin-like activity associated with C. gigantea plant parts which may serve as a promising source of vegetable milk coagulant. © Springer-Verlag Berlin Heidelberg 2014 |
abstractGer |
Abstract The steady increase in world cheese demand keeps the search for appropriate coagulating enzymes as rennet substitutes in the scientific focus. This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate. CE from latex exhibited high caseinolytic (86.445 ± 1.055 U/ml) as well as milk-clotting activity (450 U/ml) when compared to other parts. Significant milk clotting index (MCI) was presented by crude enzyme of latex followed by stem, flower and leaf in the decreasing order (p < 0.05). CE from all parts showed an optimum activity at 37 °C, pH 5.5 and 10 mM calcium chloride concentration with excellent pH (4.5–6.5) and thermal stability (30–60 °C). Hydrolysis pattern of casein components by CE during 1 h incubation, as assessed by Tricine–SDS-PAGE, and subsequent peak analysis revealed CE from stem to be closely similar to that of rennin. However, extensive casein hydrolysis was observed when incubated with crude latex enzyme. Casein bands of CE and rennin tended to disappear as incubation progressed to 24 h. Proteolytic degradation was found to be advanced and resulted in complete breakdown of casein fractions unravelling the importance of incubation time as a possible essential requisite for controlled and appropriate casein hydrolysis. The study provides evidence of rennin-like activity associated with C. gigantea plant parts which may serve as a promising source of vegetable milk coagulant. © Springer-Verlag Berlin Heidelberg 2014 |
abstract_unstemmed |
Abstract The steady increase in world cheese demand keeps the search for appropriate coagulating enzymes as rennet substitutes in the scientific focus. This work reports the milk-clotting activities of aqueous crude enzyme (CE) from different parts of Calotropis gigantea using skim milk as substrate. CE from latex exhibited high caseinolytic (86.445 ± 1.055 U/ml) as well as milk-clotting activity (450 U/ml) when compared to other parts. Significant milk clotting index (MCI) was presented by crude enzyme of latex followed by stem, flower and leaf in the decreasing order (p < 0.05). CE from all parts showed an optimum activity at 37 °C, pH 5.5 and 10 mM calcium chloride concentration with excellent pH (4.5–6.5) and thermal stability (30–60 °C). Hydrolysis pattern of casein components by CE during 1 h incubation, as assessed by Tricine–SDS-PAGE, and subsequent peak analysis revealed CE from stem to be closely similar to that of rennin. However, extensive casein hydrolysis was observed when incubated with crude latex enzyme. Casein bands of CE and rennin tended to disappear as incubation progressed to 24 h. Proteolytic degradation was found to be advanced and resulted in complete breakdown of casein fractions unravelling the importance of incubation time as a possible essential requisite for controlled and appropriate casein hydrolysis. The study provides evidence of rennin-like activity associated with C. gigantea plant parts which may serve as a promising source of vegetable milk coagulant. © Springer-Verlag Berlin Heidelberg 2014 |
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title_short |
Characterisation of potential milk coagulants from Calotropis gigantea plant parts and their hydrolytic pattern of bovine casein |
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https://dx.doi.org/10.1007/s00217-014-2177-0 |
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Singh, Maheshwari Kumari Bindhu, O. S. |
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doi_str |
10.1007/s00217-014-2177-0 |
up_date |
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score |
7.401532 |