메뉴 건너뛰기




Volumn 245, Issue 3, 2019, Pages 535-544

Purification and identification of peptides with high angiotensin-I converting enzyme (ACE) inhibitory activity from honeybee pupae (Apis mellifera) hydrolysates with in silico gastrointestinal digestion

Author keywords

ACE inhibitory activity; Enzymatic hydrolysates; Functional food; Gastrointestinal digestion; Honeybee pupae

Indexed keywords

BIOLOGICAL MATERIALS; FILTRATION; FUNCTIONAL FOOD; GEL PERMEATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PURIFICATION;

EID: 85060326949     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-018-03223-7     Document Type: Article
Times cited : (16)

References (38)
  • 2
    • 85028919846 scopus 로고    scopus 로고
    • Unlocking the biological potential of proteins from edible insects through enzymatic hydrolysis: a review
    • Nongonierma AB, FitzGerald RJ (2017) Unlocking the biological potential of proteins from edible insects through enzymatic hydrolysis: a review. Innov Food Sci Emerg 43:239–252
    • (2017) Innov Food Sci Emerg , vol.43 , pp. 239-252
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 5
    • 84978896460 scopus 로고    scopus 로고
    • Insects: a protein-rich feed ingredient in pig and poultry diets
    • Veldkamp T, Bosch G (2015) Insects: a protein-rich feed ingredient in pig and poultry diets. Anim Front 5:45–50
    • (2015) Anim Front , vol.5 , pp. 45-50
    • Veldkamp, T.1    Bosch, G.2
  • 7
    • 46849108707 scopus 로고    scopus 로고
    • Purification and identification of an angiotensin I converting enzyme (ACE) inhibitory peptide from the gastrointestinal hydrolysate of the cotton leafworm, Spodoptera littoralis
    • Vercruysse L, Smagghe G, Matsui T, Van Camp J (2008) Purification and identification of an angiotensin I converting enzyme (ACE) inhibitory peptide from the gastrointestinal hydrolysate of the cotton leafworm, Spodoptera littoralis. Process Biochem 43:900–904
    • (2008) Process Biochem , vol.43 , pp. 900-904
    • Vercruysse, L.1    Smagghe, G.2    Matsui, T.3    Van Camp, J.4
  • 8
    • 85032728194 scopus 로고    scopus 로고
    • Graphitized porous carbon for rapid screening of angiotensin-converting enzymeinhibitory peptide GAMVVH from silkworm pupa protein and molecular insight into inhibition mechanism
    • Tao M, Sun H, Liu L, Luo X, Lin G, Li R, Zhao Z, Zhao Z (2017) Graphitized porous carbon for rapid screening of angiotensin-converting enzymeinhibitory peptide GAMVVH from silkworm pupa protein and molecular insight into inhibition mechanism. J Agric Food Chem 65:8626–8633
    • (2017) J Agric Food Chem , vol.65 , pp. 8626-8633
    • Tao, M.1    Sun, H.2    Liu, L.3    Luo, X.4    Lin, G.5    Li, R.6    Zhao, Z.7    Zhao, Z.8
  • 9
    • 84875375739 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme (ACE) inhibitory peptide derived from Tenebrio molitor (L.) larva protein hydrolysate
    • Dai C, Ma H, Luo L, Yin X (2013) Angiotensin I-converting enzyme (ACE) inhibitory peptide derived from Tenebrio molitor (L.) larva protein hydrolysate. Eur Food Res Technol 236:681–689
    • (2013) Eur Food Res Technol , vol.236 , pp. 681-689
    • Dai, C.1    Ma, H.2    Luo, L.3    Yin, X.4
  • 11
    • 77952564007 scopus 로고    scopus 로고
    • Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: prospects in the pharmaceutical industry
    • Wijesekara I, Kim SK (2010) Angiotensin-I-converting enzyme (ACE) inhibitors from marine resources: prospects in the pharmaceutical industry. Mar Drugs 8:1080–1093
    • (2010) Mar Drugs , vol.8 , pp. 1080-1093
    • Wijesekara, I.1    Kim, S.K.2
  • 12
    • 77957016710 scopus 로고    scopus 로고
    • Production of enzymatic hydrolysates with antioxidant and angiotensin-I converting enzyme inhibitory activity from pumpkin oil cake protein isolate
    • Vaštag Ž, Popović L, Popović S, Krimer V, Peričin D (2011) Production of enzymatic hydrolysates with antioxidant and angiotensin-I converting enzyme inhibitory activity from pumpkin oil cake protein isolate. Food Chem 124:1316–1321
    • (2011) Food Chem , vol.124 , pp. 1316-1321
    • Vaštag, Ž.1    Popović, L.2    Popović, S.3    Krimer, V.4    Peričin, D.5
  • 13
    • 84967313048 scopus 로고    scopus 로고
    • Nutritional value and chemical composition of larvae, pupae, and adults of worker honey bee, Apis mellifera ligustica as a sustainable food source
    • Ghosh S, Jung C, Meyer-Rochow VB (2016) Nutritional value and chemical composition of larvae, pupae, and adults of worker honey bee, Apis mellifera ligustica as a sustainable food source. J Asia-Pac Entomol l19:487–495
    • (2016) J Asia-Pac Entomol , vol.l19 , pp. 487-495
    • Ghosh, S.1    Jung, C.2    Meyer-Rochow, V.B.3
  • 14
    • 84866062844 scopus 로고    scopus 로고
    • Western honeybee drones and workers (Apis mellifera ligustica) have different olfactory mechanisms than eastern honeybees (Apis cerana cerana)
    • Woltedji D, Song F, Zhang L, Gala A, Han B, Feng M, Fang Y, Li J (2012) Western honeybee drones and workers (Apis mellifera ligustica) have different olfactory mechanisms than eastern honeybees (Apis cerana cerana). J Proteome Res 11:4526–4540
    • (2012) J Proteome Res , vol.11 , pp. 4526-4540
    • Woltedji, D.1    Song, F.2    Zhang, L.3    Gala, A.4    Han, B.5    Feng, M.6    Fang, Y.7    Li, J.8
  • 16
    • 84876440123 scopus 로고    scopus 로고
    • Nutritional composition and safety aspects of edible insects
    • Rumpold BA, Schluter OK (2013) Nutritional composition and safety aspects of edible insects. Mol Nutr Food Res 57:802–823
    • (2013) Mol Nutr Food Res , vol.57 , pp. 802-823
    • Rumpold, B.A.1    Schluter, O.K.2
  • 18
    • 34548284434 scopus 로고    scopus 로고
    • Antioxidant and free radical-scavenging activities of chickpea protein hydrolysate (CPH)
    • Li Y, Jiang B, Zhang T, Mu W, Liu J (2008) Antioxidant and free radical-scavenging activities of chickpea protein hydrolysate (CPH). Food Chem 106:444–450
    • (2008) Food Chem , vol.106 , pp. 444-450
    • Li, Y.1    Jiang, B.2    Zhang, T.3    Mu, W.4    Liu, J.5
  • 19
    • 84907685485 scopus 로고    scopus 로고
    • Stability of casein antioxidant peptide fractions during in vitro digestion/Caco-2 cell model: characteristics of the resistant peptides
    • Xie N, Liu S, Wang C, Li B (2014) Stability of casein antioxidant peptide fractions during in vitro digestion/Caco-2 cell model: characteristics of the resistant peptides. Eur Food Res Technol 239:577–586
    • (2014) Eur Food Res Technol , vol.239 , pp. 577-586
    • Xie, N.1    Liu, S.2    Wang, C.3    Li, B.4
  • 20
    • 0017645560 scopus 로고
    • Sensitive fluorimetric assay for serum angiotensin-converting enzyme with natural substrate angiotensin-1
    • Friedland J, Silverstein E (1977) Sensitive fluorimetric assay for serum angiotensin-converting enzyme with natural substrate angiotensin-1. Am J Clin Pathol 68:225–228
    • (1977) Am J Clin Pathol , vol.68 , pp. 225-228
    • Friedland, J.1    Silverstein, E.2
  • 21
    • 84969522235 scopus 로고    scopus 로고
    • Modified spectrophotometric method for assay of angiotensin I-converting enzyme inhibitory activity of food-derived peptides
    • Gao D, Cao Y, Mai X (2011) Modified spectrophotometric method for assay of angiotensin I-converting enzyme inhibitory activity of food-derived peptides. J Zhejiang Univ 37:219–223
    • (2011) J Zhejiang Univ , vol.37 , pp. 219-223
    • Gao, D.1    Cao, Y.2    Mai, X.3
  • 22
    • 84949571035 scopus 로고    scopus 로고
    • Production of ACE inhibitory peptides from sweet sorghum grain protein using alcalase: hydrolysis kinetic, purification and molecular docking study
    • Wu Q, Du J, Jia J, Kuang C (2016) Production of ACE inhibitory peptides from sweet sorghum grain protein using alcalase: hydrolysis kinetic, purification and molecular docking study. Food Chem 199:140–149
    • (2016) Food Chem , vol.199 , pp. 140-149
    • Wu, Q.1    Du, J.2    Jia, J.3    Kuang, C.4
  • 23
    • 85019740096 scopus 로고    scopus 로고
    • Production and identification of antioxidant and angiotensin-converting enzyme inhibition and dipeptidyl peptidase IV inhibitory peptides from bighead carp (Hypophthalmichthys nobilis) muscle hydrolysate
    • Zhang C, Zhang Y, Wang Z, Chen S, Luo Y (2017) Production and identification of antioxidant and angiotensin-converting enzyme inhibition and dipeptidyl peptidase IV inhibitory peptides from bighead carp (Hypophthalmichthys nobilis) muscle hydrolysate. J Funct Foods 35:224–235
    • (2017) J Funct Foods , vol.35 , pp. 224-235
    • Zhang, C.1    Zhang, Y.2    Wang, Z.3    Chen, S.4    Luo, Y.5
  • 24
    • 84920720891 scopus 로고    scopus 로고
    • Isolation and characterization of three antioxidant peptides from protein hydrolysate of bluefin leatherjacket (Navodon septentrionalis) heads
    • Chi C-F, Wang B, Wang Y-M, Zhang B, Deng S-G (2015) Isolation and characterization of three antioxidant peptides from protein hydrolysate of bluefin leatherjacket (Navodon septentrionalis) heads. J Funct Foods 12:1–10
    • (2015) J Funct Foods , vol.12 , pp. 1-10
    • Chi, C.-F.1    Wang, B.2    Wang, Y.-M.3    Zhang, B.4    Deng, S.-G.5
  • 25
    • 0034840775 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate
    • Kim S, Byun H, Park P, Shahidi F (2001) Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate. J Agric Food Chem 49:2992–2996
    • (2001) J Agric Food Chem , vol.49 , pp. 2992-2996
    • Kim, S.1    Byun, H.2    Park, P.3    Shahidi, F.4
  • 26
    • 84855819460 scopus 로고    scopus 로고
    • Purification and characterization of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide derived from enzymatic hydrolysate of grass carp protein
    • Chen J, Wang Y, Zhong Q, Wu Y, Xia W (2012) Purification and characterization of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide derived from enzymatic hydrolysate of grass carp protein. Peptides 33:52–58
    • (2012) Peptides , vol.33 , pp. 52-58
    • Chen, J.1    Wang, Y.2    Zhong, Q.3    Wu, Y.4    Xia, W.5
  • 27
    • 13444252962 scopus 로고    scopus 로고
    • Fractionation of angiotensin I converting enzyme inhibitory activity from pea and whey proteinin vitro gastrointestinal digests
    • Vermeirssen V, Van Camp J, Verstraete W (2005) Fractionation of angiotensin I converting enzyme inhibitory activity from pea and whey proteinin vitro gastrointestinal digests. J Sci Food Agric 85:399–405
    • (2005) J Sci Food Agric , vol.85 , pp. 399-405
    • Vermeirssen, V.1    Van Camp, J.2    Verstraete, W.3
  • 29
    • 84898024608 scopus 로고    scopus 로고
    • Purification and identification of antioxidant peptides from sweet potato protein hydrolysates by Alcalase
    • Zhang M, Mu T-H, Sun M-J (2014) Purification and identification of antioxidant peptides from sweet potato protein hydrolysates by Alcalase. J Funct Foods 7:191–200
    • (2014) J Funct Foods , vol.7 , pp. 191-200
    • Zhang, M.1    Mu, T.-H.2    Sun, M.-J.3
  • 30
    • 85009343254 scopus 로고    scopus 로고
    • Purification, modification and inhibition mechanism of angiotensin I-converting enzyme inhibitory peptide from silkworm pupa (Bombyx mori) protein hydrolysate
    • Tao M, Wang C, Liao D, Liu H, Zhao Z, Zhao Z (2017) Purification, modification and inhibition mechanism of angiotensin I-converting enzyme inhibitory peptide from silkworm pupa (Bombyx mori) protein hydrolysate. Process Biochem 54:172–179
    • (2017) Process Biochem , vol.54 , pp. 172-179
    • Tao, M.1    Wang, C.2    Liao, D.3    Liu, H.4    Zhao, Z.5    Zhao, Z.6
  • 31
    • 44249117319 scopus 로고    scopus 로고
    • ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)
    • Tsai J-S, Chen J-L, Pan BS (2008) ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria). Process Biochem 43:743–747
    • (2008) Process Biochem , vol.43 , pp. 743-747
    • Tsai, J.-S.1    Chen, J.-L.2    Pan, B.S.3
  • 32
    • 84887192119 scopus 로고    scopus 로고
    • Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC–MS/MS
    • Lau CC, Abdullah N, Shuib AS, Aminudin N (2014) Novel angiotensin I-converting enzyme inhibitory peptides derived from edible mushroom Agaricus bisporus (J.E. Lange) Imbach identified by LC–MS/MS. Food Chem 148:396–401
    • (2014) Food Chem , vol.148 , pp. 396-401
    • Lau, C.C.1    Abdullah, N.2    Shuib, A.S.3    Aminudin, N.4
  • 33
    • 0029286291 scopus 로고
    • Purification and characterization of angiotensin I-converting enzyme-inhibitors from sour milk
    • Nakamura Y, Yamamoto N, Sakai K, Okubo A, Yamazaki S, Takano T (1995) Purification and characterization of angiotensin I-converting enzyme-inhibitors from sour milk. J Dairy Sci 78:777–783
    • (1995) J Dairy Sci , vol.78 , pp. 777-783
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Okubo, A.4    Yamazaki, S.5    Takano, T.6
  • 34
    • 84992679420 scopus 로고    scopus 로고
    • Identification, functional gastrointestinal stability and molecular docking studies of lentil peptides with dual antioxidant and angiotensin I converting enzyme inhibitory activities
    • Garcia-Mora P, Martin-Martinez M, Angeles Bonache M, Gonzalez-Muniz R, Penas E, Frias J, Martinez-Villaluenga C (2017) Identification, functional gastrointestinal stability and molecular docking studies of lentil peptides with dual antioxidant and angiotensin I converting enzyme inhibitory activities. Food Chem 221:464–472
    • (2017) Food Chem , vol.221 , pp. 464-472
    • Garcia-Mora, P.1    Martin-Martinez, M.2    Angeles Bonache, M.3    Gonzalez-Muniz, R.4    Penas, E.5    Frias, J.6    Martinez-Villaluenga, C.7
  • 35
    • 0034951098 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin
    • Byun H, Kim S (2001) Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin. Process Biochem 36:1155–1162
    • (2001) Process Biochem , vol.36 , pp. 1155-1162
    • Byun, H.1    Kim, S.2
  • 36
    • 84990847757 scopus 로고    scopus 로고
    • Bioavailability of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from Virgibacillus halodenitrificans SK1-3-7 proteinases hydrolyzed tilapia muscle proteins
    • Toopcham T, Mes JJ, Wichers HJ, Roytrakul S, Yongsawatdigul J (2017) Bioavailability of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from Virgibacillus halodenitrificans SK1-3-7 proteinases hydrolyzed tilapia muscle proteins. Food Chem 220:190–197
    • (2017) Food Chem , vol.220 , pp. 190-197
    • Toopcham, T.1    Mes, J.J.2    Wichers, H.J.3    Roytrakul, S.4    Yongsawatdigul, J.5
  • 37
    • 84963568271 scopus 로고    scopus 로고
    • Revalorisation of bovine collagen as a potential precursor of angiotensin I-converting enzyme (ACE) inhibitory peptides based on in silico and in vitro protein digestions
    • Fu Y, Young JF, Løkke MM, Lametsch R, Aluko RE, Therkildsen M (2016) Revalorisation of bovine collagen as a potential precursor of angiotensin I-converting enzyme (ACE) inhibitory peptides based on in silico and in vitro protein digestions. J Funct Foods 24:196–206
    • (2016) J Funct Foods , vol.24 , pp. 196-206
    • Fu, Y.1    Young, J.F.2    Løkke, M.M.3    Lametsch, R.4    Aluko, R.E.5    Therkildsen, M.6
  • 38
    • 84897110510 scopus 로고    scopus 로고
    • Bioinformatics approaches, prospects and challenges of food bioactive peptide research
    • Udenigwe CC (2014) Bioinformatics approaches, prospects and challenges of food bioactive peptide research. Trends Food Sci Technol 36:137–143
    • (2014) Trends Food Sci Technol , vol.36 , pp. 137-143
    • Udenigwe, C.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.