Production and characterization of angiotensin converting enzyme (ACE) inhibitory peptides from apricot (Prunus armeniaca L.) kernel protein hydrolysate
Six different proteases (Flavourzyme®, Neutrase®, Protamex®, Alcalase® 2.4L, Proleather® FG-F, and papain) were employed to hydrolyze apricot kernel protein (AKP). Alcalase® is an inexpensive and non-specific protease that has been shown to be useful for the generation of bioactive peptides from AKP...
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| Veröffentlicht in: | European food research & technology 2010-05, Vol.231 (1), p.13-19 |
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| creator | Zhu, Zhenbao Qiu, Nongxue Yi, Jianhua |
| description | Six different proteases (Flavourzyme®, Neutrase®, Protamex®, Alcalase® 2.4L, Proleather® FG-F, and papain) were employed to hydrolyze apricot kernel protein (AKP). Alcalase® is an inexpensive and non-specific protease that has been shown to be useful for the generation of bioactive peptides from AKP. Alcalase® 2.4L was selected for further study on enzymatic preparation of ACE inhibitory peptide from AKP. After 60-min hydrolysis, the highest ACE inhibition was 82 ± 0.14%. Results of molecular weight distribution revealed that most of ACE inhibition activity was probably attributed to low-molecular weight peptide fraction ranging from 200 to 900 Da. Ultrafiltration on membranes with several molecular weight cutoffs (MWCFs) demonstrated that most of the ACE inhibitory activity was due to peptides with a less than 1,000 Da molecular weight: the IC₅₀ value of the 1-kDa ultrafiltrate was 0.15 ± 0.007 mg mL⁻¹, while it was 0.378 ± 0.015 mg mL⁻¹ before ultrafiltration. Additionally, further separation and purification of the ACE inhibitory peptides were carried out using gel filtration and C₁₈ RP-HPLC. The result of research can be used to optimize AKP enzymatic hydrolysis for producing ACE inhibitory peptides which could be used for food industry and nutraceuticals. |
| doi_str_mv | 10.1007/s00217-010-1235-5 |
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Alcalase® is an inexpensive and non-specific protease that has been shown to be useful for the generation of bioactive peptides from AKP. Alcalase® 2.4L was selected for further study on enzymatic preparation of ACE inhibitory peptide from AKP. After 60-min hydrolysis, the highest ACE inhibition was 82 ± 0.14%. Results of molecular weight distribution revealed that most of ACE inhibition activity was probably attributed to low-molecular weight peptide fraction ranging from 200 to 900 Da. Ultrafiltration on membranes with several molecular weight cutoffs (MWCFs) demonstrated that most of the ACE inhibitory activity was due to peptides with a less than 1,000 Da molecular weight: the IC₅₀ value of the 1-kDa ultrafiltrate was 0.15 ± 0.007 mg mL⁻¹, while it was 0.378 ± 0.015 mg mL⁻¹ before ultrafiltration. Additionally, further separation and purification of the ACE inhibitory peptides were carried out using gel filtration and C₁₈ RP-HPLC. The result of research can be used to optimize AKP enzymatic hydrolysis for producing ACE inhibitory peptides which could be used for food industry and nutraceuticals.</description><identifier>ISSN: 1438-2377</identifier><identifier>EISSN: 1438-2385</identifier><identifier>DOI: 10.1007/s00217-010-1235-5</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>Agriculture ; Analytical Chemistry ; Antihypertensives ; Biological and medical sciences ; Biotechnology ; Cardiovascular disease ; Chemistry ; Chemistry and Materials Science ; Enzymes ; Food ; Food industries ; Food Science ; Forestry ; Fruit and vegetable industries ; Fruits ; Functional foods & nutraceuticals ; Fundamental and applied biological sciences. Psychology ; Hydrolysis ; Hypertension ; Life sciences ; Liquid chromatography ; Molecular weight ; Nutrition ; Original Paper ; Peptides ; Proteins ; Statistical analysis ; Ultrafiltration</subject><ispartof>European food research & technology, 2010-05, Vol.231 (1), p.13-19</ispartof><rights>Springer-Verlag 2010</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c369t-14b2483110755098f0f6cf544b509ac2d93ec47e071ae7e234eb92255b6a9a33</citedby><cites>FETCH-LOGICAL-c369t-14b2483110755098f0f6cf544b509ac2d93ec47e071ae7e234eb92255b6a9a33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00217-010-1235-5$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00217-010-1235-5$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22656396$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhu, Zhenbao</creatorcontrib><creatorcontrib>Qiu, Nongxue</creatorcontrib><creatorcontrib>Yi, Jianhua</creatorcontrib><title>Production and characterization of angiotensin converting enzyme (ACE) inhibitory peptides from apricot (Prunus armeniaca L.) kernel protein hydrolysate</title><title>European food research & technology</title><addtitle>Eur Food Res Technol</addtitle><description>Six different proteases (Flavourzyme®, Neutrase®, Protamex®, Alcalase® 2.4L, Proleather® FG-F, and papain) were employed to hydrolyze apricot kernel protein (AKP). Alcalase® is an inexpensive and non-specific protease that has been shown to be useful for the generation of bioactive peptides from AKP. Alcalase® 2.4L was selected for further study on enzymatic preparation of ACE inhibitory peptide from AKP. After 60-min hydrolysis, the highest ACE inhibition was 82 ± 0.14%. Results of molecular weight distribution revealed that most of ACE inhibition activity was probably attributed to low-molecular weight peptide fraction ranging from 200 to 900 Da. Ultrafiltration on membranes with several molecular weight cutoffs (MWCFs) demonstrated that most of the ACE inhibitory activity was due to peptides with a less than 1,000 Da molecular weight: the IC₅₀ value of the 1-kDa ultrafiltrate was 0.15 ± 0.007 mg mL⁻¹, while it was 0.378 ± 0.015 mg mL⁻¹ before ultrafiltration. Additionally, further separation and purification of the ACE inhibitory peptides were carried out using gel filtration and C₁₈ RP-HPLC. The result of research can be used to optimize AKP enzymatic hydrolysis for producing ACE inhibitory peptides which could be used for food industry and nutraceuticals.</description><subject>Agriculture</subject><subject>Analytical Chemistry</subject><subject>Antihypertensives</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cardiovascular disease</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Enzymes</subject><subject>Food</subject><subject>Food industries</subject><subject>Food Science</subject><subject>Forestry</subject><subject>Fruit and vegetable industries</subject><subject>Fruits</subject><subject>Functional foods & nutraceuticals</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrolysis</subject><subject>Hypertension</subject><subject>Life sciences</subject><subject>Liquid chromatography</subject><subject>Molecular weight</subject><subject>Nutrition</subject><subject>Original Paper</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Statistical analysis</subject><subject>Ultrafiltration</subject><issn>1438-2377</issn><issn>1438-2385</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kd1u1DAQhSMEEqXwAFxhISG1Fyn-zc9ltSot0kpUolxHE2ey67JrL2OnUvokPC5eUpU7ruwZn_N5fFwU7wW_EJzXnyPnUtQlF7wUUpnSvChOhFZNKVVjXj7v6_p18SbGe85NWwl9Uvy-pTBMNrngGfiB2S0Q2ITkHuFvM4y5v3EhoY_OMxv8A1JyfsPQP857ZGeXq6tz5vzW9S4FmtkBD8kNGNlIYc_gQM6GxM5uafJTZEB79A4ssPXFOfuJ5HHHDpT5mb6dBwq7OULCt8WrEXYR3z2tp8Xdl6u71U25_nb9dXW5Lq2q2lQK3UvdKCF4bQxvm5GPlR2N1n2uwMqhVWh1jbwWgDVKpbFvpTSmr6AFpU6Ljws2j_Brwpi6-zCRzzd2kpum0q2sskgsIkshRsKxy4_aA82d4N0x_m6Jv-PHOsffmez59ASGaGE3Enjr4rNRyspUqj2y5aKL-chvkP4N8D_4h8U0QuhgQxn847vkQnHRyPyxSv0BE1ygGg</recordid><startdate>20100501</startdate><enddate>20100501</enddate><creator>Zhu, Zhenbao</creator><creator>Qiu, Nongxue</creator><creator>Yi, Jianhua</creator><general>Berlin/Heidelberg : Springer-Verlag</general><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QO</scope><scope>7QR</scope><scope>7RQ</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X2</scope><scope>7XB</scope><scope>87Z</scope><scope>88I</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FK</scope><scope>8FL</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>F~G</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>L.-</scope><scope>L6V</scope><scope>M0C</scope><scope>M0K</scope><scope>M2P</scope><scope>M7S</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope></search><sort><creationdate>20100501</creationdate><title>Production and characterization of angiotensin converting enzyme (ACE) inhibitory peptides from apricot (Prunus armeniaca L.) kernel protein hydrolysate</title><author>Zhu, Zhenbao ; Qiu, Nongxue ; Yi, Jianhua</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c369t-14b2483110755098f0f6cf544b509ac2d93ec47e071ae7e234eb92255b6a9a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Agriculture</topic><topic>Analytical Chemistry</topic><topic>Antihypertensives</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cardiovascular disease</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Enzymes</topic><topic>Food</topic><topic>Food industries</topic><topic>Food Science</topic><topic>Forestry</topic><topic>Fruit and vegetable industries</topic><topic>Fruits</topic><topic>Functional foods & nutraceuticals</topic><topic>Fundamental and applied biological sciences. 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Alcalase® is an inexpensive and non-specific protease that has been shown to be useful for the generation of bioactive peptides from AKP. Alcalase® 2.4L was selected for further study on enzymatic preparation of ACE inhibitory peptide from AKP. After 60-min hydrolysis, the highest ACE inhibition was 82 ± 0.14%. Results of molecular weight distribution revealed that most of ACE inhibition activity was probably attributed to low-molecular weight peptide fraction ranging from 200 to 900 Da. Ultrafiltration on membranes with several molecular weight cutoffs (MWCFs) demonstrated that most of the ACE inhibitory activity was due to peptides with a less than 1,000 Da molecular weight: the IC₅₀ value of the 1-kDa ultrafiltrate was 0.15 ± 0.007 mg mL⁻¹, while it was 0.378 ± 0.015 mg mL⁻¹ before ultrafiltration. Additionally, further separation and purification of the ACE inhibitory peptides were carried out using gel filtration and C₁₈ RP-HPLC. The result of research can be used to optimize AKP enzymatic hydrolysis for producing ACE inhibitory peptides which could be used for food industry and nutraceuticals.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><doi>10.1007/s00217-010-1235-5</doi><tpages>7</tpages></addata></record> |
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| subjects | Agriculture Analytical Chemistry Antihypertensives Biological and medical sciences Biotechnology Cardiovascular disease Chemistry Chemistry and Materials Science Enzymes Food Food industries Food Science Forestry Fruit and vegetable industries Fruits Functional foods & nutraceuticals Fundamental and applied biological sciences. Psychology Hydrolysis Hypertension Life sciences Liquid chromatography Molecular weight Nutrition Original Paper Peptides Proteins Statistical analysis Ultrafiltration |
| title | Production and characterization of angiotensin converting enzyme (ACE) inhibitory peptides from apricot (Prunus armeniaca L.) kernel protein hydrolysate |
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