Effects of maltogenic amylase from
Maltogenic amylase originated from Lactobacillus plantarum (LpMA) was studied to investigate its applicability as an antistaling enzyme. The differential scanning calorimetry (DSC) results demonstrated that the bread treated with purified LpMA exhibited a retrogradation peak that was 65% that of the...
Ausführliche Beschreibung
Autor*in: |
Woo, Seung-Hye [verfasserIn] Shin, Yu-Jeong [verfasserIn] Jeong, Hyun-Mo [verfasserIn] Kim, Ji-Soo [verfasserIn] Ko, Dam-Seul [verfasserIn] Hong, Jung Sun [verfasserIn] Choi, Hee-Don [verfasserIn] Shim, Jae-Hoon [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2020 |
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Schlagwörter: |
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Übergeordnetes Werk: |
Enthalten in: Journal of cereal science - London : Academic Press, 1983, 93 |
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Übergeordnetes Werk: |
volume:93 |
DOI / URN: |
10.1016/j.jcs.2020.102976 |
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Katalog-ID: |
ELV004148975 |
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520 | |a Maltogenic amylase originated from Lactobacillus plantarum (LpMA) was studied to investigate its applicability as an antistaling enzyme. The differential scanning calorimetry (DSC) results demonstrated that the bread treated with purified LpMA exhibited a retrogradation peak that was 65% that of the control bread. Then, for the purpose of practically using L. plantarum as an antistaling agent, the expression of LpMA in L. plantarum was enhanced by growth on a modified medium; the LpMA expression of L. plantarum grown on De Man, Rogosa and Sharpe (MRS) medium supplemented with an additional 6% glucose was 54 times higher than that of L. plantarum grown on the original MRS medium. The side chain length distribution analysis showed that the cell extract of L. plantarum (CELP) tended to prefer to hydrolyzes the long side chains of amylopectin (>30). During storage for 9 days at 4 °C, the bread treated with CELP exhibited a 25% slower retrogradation rate and 63% lower hardness relative to the control bread, indicating that the CELP is a potential candidate for use as an antistaling agent. | ||
650 | 4 | |a Maltogenic amylase originated from | |
650 | 4 | |a Glucose | |
650 | 4 | |a Crude enzyme | |
650 | 4 | |a Antistaling | |
700 | 1 | |a Shin, Yu-Jeong |e verfasserin |4 aut | |
700 | 1 | |a Jeong, Hyun-Mo |e verfasserin |4 aut | |
700 | 1 | |a Kim, Ji-Soo |e verfasserin |4 aut | |
700 | 1 | |a Ko, Dam-Seul |e verfasserin |4 aut | |
700 | 1 | |a Hong, Jung Sun |e verfasserin |4 aut | |
700 | 1 | |a Choi, Hee-Don |e verfasserin |4 aut | |
700 | 1 | |a Shim, Jae-Hoon |e verfasserin |4 aut | |
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2020 |
allfields |
10.1016/j.jcs.2020.102976 doi (DE-627)ELV004148975 (ELSEVIER)S0733-5210(20)30006-0 DE-627 ger DE-627 rda eng 630 640 660 DE-600 48.50 bkl 58.34 bkl Woo, Seung-Hye verfasserin aut Effects of maltogenic amylase from 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Maltogenic amylase originated from Lactobacillus plantarum (LpMA) was studied to investigate its applicability as an antistaling enzyme. The differential scanning calorimetry (DSC) results demonstrated that the bread treated with purified LpMA exhibited a retrogradation peak that was 65% that of the control bread. Then, for the purpose of practically using L. plantarum as an antistaling agent, the expression of LpMA in L. plantarum was enhanced by growth on a modified medium; the LpMA expression of L. plantarum grown on De Man, Rogosa and Sharpe (MRS) medium supplemented with an additional 6% glucose was 54 times higher than that of L. plantarum grown on the original MRS medium. The side chain length distribution analysis showed that the cell extract of L. plantarum (CELP) tended to prefer to hydrolyzes the long side chains of amylopectin (>30). During storage for 9 days at 4 °C, the bread treated with CELP exhibited a 25% slower retrogradation rate and 63% lower hardness relative to the control bread, indicating that the CELP is a potential candidate for use as an antistaling agent. Maltogenic amylase originated from Glucose Crude enzyme Antistaling Shin, Yu-Jeong verfasserin aut Jeong, Hyun-Mo verfasserin aut Kim, Ji-Soo verfasserin aut Ko, Dam-Seul verfasserin aut Hong, Jung Sun verfasserin aut Choi, Hee-Don verfasserin aut Shim, Jae-Hoon verfasserin aut Enthalten in Journal of cereal science London : Academic Press, 1983 93 Online-Ressource (DE-627)266890946 (DE-600)1469001-9 (DE-576)253762944 nnns volume:93 GBV_USEFLAG_U SYSFLAG_U GBV_ELV GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 48.50 Pflanzenproduktion: Allgemeines 58.34 Lebensmitteltechnologie AR 93 |
spelling |
10.1016/j.jcs.2020.102976 doi (DE-627)ELV004148975 (ELSEVIER)S0733-5210(20)30006-0 DE-627 ger DE-627 rda eng 630 640 660 DE-600 48.50 bkl 58.34 bkl Woo, Seung-Hye verfasserin aut Effects of maltogenic amylase from 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Maltogenic amylase originated from Lactobacillus plantarum (LpMA) was studied to investigate its applicability as an antistaling enzyme. The differential scanning calorimetry (DSC) results demonstrated that the bread treated with purified LpMA exhibited a retrogradation peak that was 65% that of the control bread. Then, for the purpose of practically using L. plantarum as an antistaling agent, the expression of LpMA in L. plantarum was enhanced by growth on a modified medium; the LpMA expression of L. plantarum grown on De Man, Rogosa and Sharpe (MRS) medium supplemented with an additional 6% glucose was 54 times higher than that of L. plantarum grown on the original MRS medium. The side chain length distribution analysis showed that the cell extract of L. plantarum (CELP) tended to prefer to hydrolyzes the long side chains of amylopectin (>30). During storage for 9 days at 4 °C, the bread treated with CELP exhibited a 25% slower retrogradation rate and 63% lower hardness relative to the control bread, indicating that the CELP is a potential candidate for use as an antistaling agent. Maltogenic amylase originated from Glucose Crude enzyme Antistaling Shin, Yu-Jeong verfasserin aut Jeong, Hyun-Mo verfasserin aut Kim, Ji-Soo verfasserin aut Ko, Dam-Seul verfasserin aut Hong, Jung Sun verfasserin aut Choi, Hee-Don verfasserin aut Shim, Jae-Hoon verfasserin aut Enthalten in Journal of cereal science London : Academic Press, 1983 93 Online-Ressource (DE-627)266890946 (DE-600)1469001-9 (DE-576)253762944 nnns volume:93 GBV_USEFLAG_U SYSFLAG_U GBV_ELV GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 48.50 Pflanzenproduktion: Allgemeines 58.34 Lebensmitteltechnologie AR 93 |
allfields_unstemmed |
10.1016/j.jcs.2020.102976 doi (DE-627)ELV004148975 (ELSEVIER)S0733-5210(20)30006-0 DE-627 ger DE-627 rda eng 630 640 660 DE-600 48.50 bkl 58.34 bkl Woo, Seung-Hye verfasserin aut Effects of maltogenic amylase from 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Maltogenic amylase originated from Lactobacillus plantarum (LpMA) was studied to investigate its applicability as an antistaling enzyme. The differential scanning calorimetry (DSC) results demonstrated that the bread treated with purified LpMA exhibited a retrogradation peak that was 65% that of the control bread. Then, for the purpose of practically using L. plantarum as an antistaling agent, the expression of LpMA in L. plantarum was enhanced by growth on a modified medium; the LpMA expression of L. plantarum grown on De Man, Rogosa and Sharpe (MRS) medium supplemented with an additional 6% glucose was 54 times higher than that of L. plantarum grown on the original MRS medium. The side chain length distribution analysis showed that the cell extract of L. plantarum (CELP) tended to prefer to hydrolyzes the long side chains of amylopectin (>30). During storage for 9 days at 4 °C, the bread treated with CELP exhibited a 25% slower retrogradation rate and 63% lower hardness relative to the control bread, indicating that the CELP is a potential candidate for use as an antistaling agent. Maltogenic amylase originated from Glucose Crude enzyme Antistaling Shin, Yu-Jeong verfasserin aut Jeong, Hyun-Mo verfasserin aut Kim, Ji-Soo verfasserin aut Ko, Dam-Seul verfasserin aut Hong, Jung Sun verfasserin aut Choi, Hee-Don verfasserin aut Shim, Jae-Hoon verfasserin aut Enthalten in Journal of cereal science London : Academic Press, 1983 93 Online-Ressource (DE-627)266890946 (DE-600)1469001-9 (DE-576)253762944 nnns volume:93 GBV_USEFLAG_U SYSFLAG_U GBV_ELV GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 48.50 Pflanzenproduktion: Allgemeines 58.34 Lebensmitteltechnologie AR 93 |
allfieldsGer |
10.1016/j.jcs.2020.102976 doi (DE-627)ELV004148975 (ELSEVIER)S0733-5210(20)30006-0 DE-627 ger DE-627 rda eng 630 640 660 DE-600 48.50 bkl 58.34 bkl Woo, Seung-Hye verfasserin aut Effects of maltogenic amylase from 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Maltogenic amylase originated from Lactobacillus plantarum (LpMA) was studied to investigate its applicability as an antistaling enzyme. The differential scanning calorimetry (DSC) results demonstrated that the bread treated with purified LpMA exhibited a retrogradation peak that was 65% that of the control bread. Then, for the purpose of practically using L. plantarum as an antistaling agent, the expression of LpMA in L. plantarum was enhanced by growth on a modified medium; the LpMA expression of L. plantarum grown on De Man, Rogosa and Sharpe (MRS) medium supplemented with an additional 6% glucose was 54 times higher than that of L. plantarum grown on the original MRS medium. The side chain length distribution analysis showed that the cell extract of L. plantarum (CELP) tended to prefer to hydrolyzes the long side chains of amylopectin (>30). During storage for 9 days at 4 °C, the bread treated with CELP exhibited a 25% slower retrogradation rate and 63% lower hardness relative to the control bread, indicating that the CELP is a potential candidate for use as an antistaling agent. Maltogenic amylase originated from Glucose Crude enzyme Antistaling Shin, Yu-Jeong verfasserin aut Jeong, Hyun-Mo verfasserin aut Kim, Ji-Soo verfasserin aut Ko, Dam-Seul verfasserin aut Hong, Jung Sun verfasserin aut Choi, Hee-Don verfasserin aut Shim, Jae-Hoon verfasserin aut Enthalten in Journal of cereal science London : Academic Press, 1983 93 Online-Ressource (DE-627)266890946 (DE-600)1469001-9 (DE-576)253762944 nnns volume:93 GBV_USEFLAG_U SYSFLAG_U GBV_ELV GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 48.50 Pflanzenproduktion: Allgemeines 58.34 Lebensmitteltechnologie AR 93 |
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10.1016/j.jcs.2020.102976 doi (DE-627)ELV004148975 (ELSEVIER)S0733-5210(20)30006-0 DE-627 ger DE-627 rda eng 630 640 660 DE-600 48.50 bkl 58.34 bkl Woo, Seung-Hye verfasserin aut Effects of maltogenic amylase from 2020 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Maltogenic amylase originated from Lactobacillus plantarum (LpMA) was studied to investigate its applicability as an antistaling enzyme. The differential scanning calorimetry (DSC) results demonstrated that the bread treated with purified LpMA exhibited a retrogradation peak that was 65% that of the control bread. Then, for the purpose of practically using L. plantarum as an antistaling agent, the expression of LpMA in L. plantarum was enhanced by growth on a modified medium; the LpMA expression of L. plantarum grown on De Man, Rogosa and Sharpe (MRS) medium supplemented with an additional 6% glucose was 54 times higher than that of L. plantarum grown on the original MRS medium. The side chain length distribution analysis showed that the cell extract of L. plantarum (CELP) tended to prefer to hydrolyzes the long side chains of amylopectin (>30). During storage for 9 days at 4 °C, the bread treated with CELP exhibited a 25% slower retrogradation rate and 63% lower hardness relative to the control bread, indicating that the CELP is a potential candidate for use as an antistaling agent. Maltogenic amylase originated from Glucose Crude enzyme Antistaling Shin, Yu-Jeong verfasserin aut Jeong, Hyun-Mo verfasserin aut Kim, Ji-Soo verfasserin aut Ko, Dam-Seul verfasserin aut Hong, Jung Sun verfasserin aut Choi, Hee-Don verfasserin aut Shim, Jae-Hoon verfasserin aut Enthalten in Journal of cereal science London : Academic Press, 1983 93 Online-Ressource (DE-627)266890946 (DE-600)1469001-9 (DE-576)253762944 nnns volume:93 GBV_USEFLAG_U SYSFLAG_U GBV_ELV GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 48.50 Pflanzenproduktion: Allgemeines 58.34 Lebensmitteltechnologie AR 93 |
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Effects of maltogenic amylase from |
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Effects of maltogenic amylase from |
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Woo, Seung-Hye Shin, Yu-Jeong Jeong, Hyun-Mo Kim, Ji-Soo Ko, Dam-Seul Hong, Jung Sun Choi, Hee-Don Shim, Jae-Hoon |
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effects of maltogenic amylase from |
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Effects of maltogenic amylase from |
abstract |
Maltogenic amylase originated from Lactobacillus plantarum (LpMA) was studied to investigate its applicability as an antistaling enzyme. The differential scanning calorimetry (DSC) results demonstrated that the bread treated with purified LpMA exhibited a retrogradation peak that was 65% that of the control bread. Then, for the purpose of practically using L. plantarum as an antistaling agent, the expression of LpMA in L. plantarum was enhanced by growth on a modified medium; the LpMA expression of L. plantarum grown on De Man, Rogosa and Sharpe (MRS) medium supplemented with an additional 6% glucose was 54 times higher than that of L. plantarum grown on the original MRS medium. The side chain length distribution analysis showed that the cell extract of L. plantarum (CELP) tended to prefer to hydrolyzes the long side chains of amylopectin (>30). During storage for 9 days at 4 °C, the bread treated with CELP exhibited a 25% slower retrogradation rate and 63% lower hardness relative to the control bread, indicating that the CELP is a potential candidate for use as an antistaling agent. |
abstractGer |
Maltogenic amylase originated from Lactobacillus plantarum (LpMA) was studied to investigate its applicability as an antistaling enzyme. The differential scanning calorimetry (DSC) results demonstrated that the bread treated with purified LpMA exhibited a retrogradation peak that was 65% that of the control bread. Then, for the purpose of practically using L. plantarum as an antistaling agent, the expression of LpMA in L. plantarum was enhanced by growth on a modified medium; the LpMA expression of L. plantarum grown on De Man, Rogosa and Sharpe (MRS) medium supplemented with an additional 6% glucose was 54 times higher than that of L. plantarum grown on the original MRS medium. The side chain length distribution analysis showed that the cell extract of L. plantarum (CELP) tended to prefer to hydrolyzes the long side chains of amylopectin (>30). During storage for 9 days at 4 °C, the bread treated with CELP exhibited a 25% slower retrogradation rate and 63% lower hardness relative to the control bread, indicating that the CELP is a potential candidate for use as an antistaling agent. |
abstract_unstemmed |
Maltogenic amylase originated from Lactobacillus plantarum (LpMA) was studied to investigate its applicability as an antistaling enzyme. The differential scanning calorimetry (DSC) results demonstrated that the bread treated with purified LpMA exhibited a retrogradation peak that was 65% that of the control bread. Then, for the purpose of practically using L. plantarum as an antistaling agent, the expression of LpMA in L. plantarum was enhanced by growth on a modified medium; the LpMA expression of L. plantarum grown on De Man, Rogosa and Sharpe (MRS) medium supplemented with an additional 6% glucose was 54 times higher than that of L. plantarum grown on the original MRS medium. The side chain length distribution analysis showed that the cell extract of L. plantarum (CELP) tended to prefer to hydrolyzes the long side chains of amylopectin (>30). During storage for 9 days at 4 °C, the bread treated with CELP exhibited a 25% slower retrogradation rate and 63% lower hardness relative to the control bread, indicating that the CELP is a potential candidate for use as an antistaling agent. |
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Effects of maltogenic amylase from |
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Shin, Yu-Jeong Jeong, Hyun-Mo Kim, Ji-Soo Ko, Dam-Seul Hong, Jung Sun Choi, Hee-Don Shim, Jae-Hoon |
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