Functional properties and biological activities of perilla seed meal protein hydrolysates obtained by using different proteolytic enzymes
In this study, we aimed to determine the potential functional properties and biological activities of the hydrolysates of perilla seed meal (PSM), which is a by-product of perilla seed oil extraction. PSM protein was hydrolyzed independently by using five proteases, and their functional and biologic...
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| Published in | Food science and biotechnology Vol. 29; no. 11; pp. 1553 - 1562 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
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Singapore
Springer Singapore
01.11.2020
Springer Nature B.V 한국식품과학회 |
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| Abstract | In this study, we aimed to determine the potential functional properties and biological activities of the hydrolysates of perilla seed meal (PSM), which is a by-product of perilla seed oil extraction. PSM protein was hydrolyzed independently by using five proteases, and their functional and biological properties were analyzed. PSM protein hydrolysate exhibited high solubility at most of the tested pH values, and the trypsin-treated hydrolysate exhibited the highest water and oil absorption capacity. The neutrase-treated hydrolysate was most effective in scavenging the 1,1-diphenyl-2-picrylhydrazine radicals, whereas the pepsin-treated hydrolysate showed the highest angiotensin I-converting enzyme inhibitory effect, and anti-inflammatory activity. Trypsin-treated hydrolysate exhibited the highest scavenging activity against of 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid radicals with the IC
50
of 109.72 µg/mL. The results of the present study suggest that the type of protease used for the treatment significantly influences the functional properties and biological activities of the resulting PSM protein hydrolysates. |
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| AbstractList | In this study, we aimed to determine the potentialfunctional properties and biological activities of thehydrolysates of perilla seed meal (PSM), which is a byproductof perilla seed oil extraction. PSM protein washydrolyzed independently by using five proteases, and theirfunctional and biological properties were analyzed. PSMprotein hydrolysate exhibited high solubility at most of thetested pH values, and the trypsin-treated hydrolysateexhibited the highest water and oil absorption capacity.
The neutrase-treated hydrolysate was most effective inscavenging the 1,1-diphenyl-2-picrylhydrazine radicals,whereas the pepsin-treated hydrolysate showed the highestangiotensin I-converting enzyme inhibitory effect, andanti-inflammatory activity. Trypsin-treated hydrolysateexhibited the highest scavenging activity against of 2,20-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid radicalswith the IC50 of 109.72 lg/mL. The results of the presentstudy suggest that the type of protease used for the treatmentsignificantly influences the functional properties andbiological activities of the resulting PSM proteinhydrolysates. KCI Citation Count: 12 In this study, we aimed to determine the potential functional properties and biological activities of the hydrolysates of perilla seed meal (PSM), which is a by-product of perilla seed oil extraction. PSM protein was hydrolyzed independently by using five proteases, and their functional and biological properties were analyzed. PSM protein hydrolysate exhibited high solubility at most of the tested pH values, and the trypsin-treated hydrolysate exhibited the highest water and oil absorption capacity. The neutrase-treated hydrolysate was most effective in scavenging the 1,1-diphenyl-2-picrylhydrazine radicals, whereas the pepsin-treated hydrolysate showed the highest angiotensin I-converting enzyme inhibitory effect, and anti-inflammatory activity. Trypsin-treated hydrolysate exhibited the highest scavenging activity against of 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid radicals with the IC of 109.72 µg/mL. The results of the present study suggest that the type of protease used for the treatment significantly influences the functional properties and biological activities of the resulting PSM protein hydrolysates. In this study, we aimed to determine the potential functional properties and biological activities of the hydrolysates of perilla seed meal (PSM), which is a by-product of perilla seed oil extraction. PSM protein was hydrolyzed independently by using five proteases, and their functional and biological properties were analyzed. PSM protein hydrolysate exhibited high solubility at most of the tested pH values, and the trypsin-treated hydrolysate exhibited the highest water and oil absorption capacity. The neutrase-treated hydrolysate was most effective in scavenging the 1,1-diphenyl-2-picrylhydrazine radicals, whereas the pepsin-treated hydrolysate showed the highest angiotensin I-converting enzyme inhibitory effect, and anti-inflammatory activity. Trypsin-treated hydrolysate exhibited the highest scavenging activity against of 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid radicals with the IC 50 of 109.72 µg/mL. The results of the present study suggest that the type of protease used for the treatment significantly influences the functional properties and biological activities of the resulting PSM protein hydrolysates. In this study, we aimed to determine the potential functional properties and biological activities of the hydrolysates of perilla seed meal (PSM), which is a by-product of perilla seed oil extraction. PSM protein was hydrolyzed independently by using five proteases, and their functional and biological properties were analyzed. PSM protein hydrolysate exhibited high solubility at most of the tested pH values, and the trypsin-treated hydrolysate exhibited the highest water and oil absorption capacity. The neutrase-treated hydrolysate was most effective in scavenging the 1,1-diphenyl-2-picrylhydrazine radicals, whereas the pepsin-treated hydrolysate showed the highest angiotensin I-converting enzyme inhibitory effect, and anti-inflammatory activity. Trypsin-treated hydrolysate exhibited the highest scavenging activity against of 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid radicals with the IC50 of 109.72 µg/mL. The results of the present study suggest that the type of protease used for the treatment significantly influences the functional properties and biological activities of the resulting PSM protein hydrolysates. |
| Author | Yoon, Kyung Young Kim, Ja Min |
| Author_xml | – sequence: 1 givenname: Ja Min surname: Kim fullname: Kim, Ja Min organization: Department of Food and Nutrition, Yeungnam University – sequence: 2 givenname: Kyung Young orcidid: 0000-0003-0626-5563 surname: Yoon fullname: Yoon, Kyung Young email: yoonky2441@ynu.ac.kr organization: Department of Food and Nutrition, Yeungnam University |
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| Cites_doi | 10.1016/j.foodres.2013.03.036 10.1007/s10068-012-0226-7 10.31883/pjfns-2019-0011 10.1016/S0308-8146(97)00199-4 10.1016/j.foodchem.2013.12.008 10.1016/j.foodres.2010.02.009 10.1016/j.jff.2015.04.023 10.1016/j.foodchem.2018.07.103 10.17221/145/2018-CJFS 10.1016/j.foodhyd.2017.01.003 10.1016/j.procbio.2005.12.029 10.1016/j.foodchem.2006.06.062 10.1111/jfbc.12571 10.1016/S0891-5849(98)00315-3 10.6090/jarq.42.211 10.1016/S0308-8146(98)00030-2 10.1016/j.jnutbio.2005.02.005 10.1007/s12562-017-1067-3 10.1016/j.jcs.2016.06.001 10.1002/fsn3.998 10.1111/j.1365-2621.2010.02219.x 10.1016/j.foodchem.2009.12.027 10.1080/10498850.2016.1221015 10.1016/j.foodchem.2008.12.019 10.1016/j.ifset.2012.07.009 10.1016/j.foodchem.2014.05.112 10.1080/10498850.2014.994083 10.1016/j.foodchem.2006.01.011 10.1016/j.supflu.2015.03.016 10.1016/j.foodres.2017.07.032 10.1016/j.jchromb.2009.11.033 10.1371/journal.pone.0200021 |
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| Keywords | Protein hydrolysate Functional property Agricultural by-product Perilla seed meal Enzymatic hydrolysis Biological activity |
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| Snippet | In this study, we aimed to determine the potential functional properties and biological activities of the hydrolysates of perilla seed meal (PSM), which is a... In this study, we aimed to determine the potentialfunctional properties and biological activities of thehydrolysates of perilla seed meal (PSM), which is a... |
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| SubjectTerms | Angiotensin Angiotensin I Anti-inflammatory agents Biological properties Chemistry Chemistry and Materials Science Food Science Hydrolysates Inflammation Nutrition Oils & fats Oilseeds Pepsin Peptidyl-dipeptidase A Proteins Proteolysis Proteolytic enzymes Radicals Scavenging Seed meal Seeds Sulfonic acid Trypsin 식품과학 |
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| Title | Functional properties and biological activities of perilla seed meal protein hydrolysates obtained by using different proteolytic enzymes |
| URI | https://link.springer.com/article/10.1007/s10068-020-00810-x https://www.ncbi.nlm.nih.gov/pubmed/33088604 https://www.proquest.com/docview/2451399426/abstract/ https://search.proquest.com/docview/2453687284 https://pubmed.ncbi.nlm.nih.gov/PMC7561629 https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART002637794 |
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