메뉴 건너뛰기




Volumn 5, Issue 4, 2017, Pages 119-126

Multifunctional biological activities of water extract of housefly larvae (Musca domestica)

Author keywords

Angiotensin converting enzyme inhibitory activity; Antioxidant activity; Decoction method; Dipeptidyl peptidase IV inhibitory activity; Housefly larvae water extract; Multifunctional activities

Indexed keywords

ANIMAL EXTRACT; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL PEPTIDASE IV; HOUSEFLY LARVAE WATER EXTRACT; UNCLASSIFIED DRUG;

EID: 85030256505     PISSN: None     EISSN: 22134344     Source Type: Journal    
DOI: 10.1016/j.phanu.2017.09.001     Document Type: Article
Times cited : (26)

References (52)
  • 1
    • 26844564082 scopus 로고    scopus 로고
    • Oxidative stress and the use of antioxidants in diabetes: linking basic science to clinical practice
    • Johansen, J.S., Harris, A.K., Rychly, D.J., Ergul, A., Oxidative stress and the use of antioxidants in diabetes: linking basic science to clinical practice. Cardiovasc. Diabetol., 4, 2005, 10.1186/1475-2840-4-5.
    • (2005) Cardiovasc. Diabetol. , vol.4
    • Johansen, J.S.1    Harris, A.K.2    Rychly, D.J.3    Ergul, A.4
  • 3
    • 84883328087 scopus 로고    scopus 로고
    • WHO, A Global Brief on Hypertension (Silent Killer, Global Public Health Crisis)
    • (Accessed 10 June 2017)
    • WHO, A Global Brief on Hypertension (Silent Killer, Global Public Health Crisis). 2013 http://ish-world.com/downloads/pdf/global_brief_hypertension.pdf, (Accessed 10 June 2017).
    • (2013)
  • 4
    • 36248931664 scopus 로고    scopus 로고
    • The renin-Angiotensin aldosterone system: pathophysiological role and pharmacologic inhibition
    • Atlas, S.A., The renin-Angiotensin aldosterone system: pathophysiological role and pharmacologic inhibition. J. Manag. Care Pharm. 13 (2007), S9–S20, 10.18553/jmcp.2007.13.s8-b.9.
    • (2007) J. Manag. Care Pharm. , vol.13 , pp. S9-S20
    • Atlas, S.A.1
  • 5
    • 77957573135 scopus 로고    scopus 로고
    • Inadequate diabetic care: global figures cry for preventive measures and personalized treatment
    • George, B., Cebioglu, M., Yeghiazaryan, K., Inadequate diabetic care: global figures cry for preventive measures and personalized treatment. EPMA J. 1 (2010), 13–18, 10.1007/s13167-010-0006-5.
    • (2010) EPMA J. , vol.1 , pp. 13-18
    • George, B.1    Cebioglu, M.2    Yeghiazaryan, K.3
  • 6
    • 78651276631 scopus 로고    scopus 로고
    • Diagnosis and classification of diabetes mellitus
    • American Diabetes Association, Diagnosis and classification of diabetes mellitus. Diabetes Care 34:Suppl. 1 (2011), S62–S69, 10.2337/dc11-S062.
    • (2011) Diabetes Care , vol.34 , pp. S62-S69
    • American Diabetes Association1
  • 7
    • 77249092557 scopus 로고    scopus 로고
    • Gliptins: a new class of oral antidiabetic agents
    • Seshadri, K.G., Kirubha, M.H.B., Gliptins: a new class of oral antidiabetic agents. Indian J. Pharm. Sci. 71 (2009), 608–614, 10.4103/0250-474X.59541.
    • (2009) Indian J. Pharm. Sci. , vol.71 , pp. 608-614
    • Seshadri, K.G.1    Kirubha, M.H.B.2
  • 8
    • 84862825466 scopus 로고    scopus 로고
    • Diabetes and hypertension: is there a common metabolic pathway?
    • Cheung, B.M.Y., Li, C., Diabetes and hypertension: is there a common metabolic pathway?. Curr. Atheroscler. Rep. 14 (2012), 160–166, 10.1007/s11883-012-0227-2.
    • (2012) Curr. Atheroscler. Rep. , vol.14 , pp. 160-166
    • Cheung, B.M.Y.1    Li, C.2
  • 9
    • 15044349115 scopus 로고    scopus 로고
    • The efficiency of multi-target drugs: the network approach might help drug design
    • Csermely, P., Ágoston, V., Pongor, S., The efficiency of multi-target drugs: the network approach might help drug design. Trends Pharmacol. Sci. 26 (2005), 178–182, 10.1016/j.tips.2005.02.007.
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 178-182
    • Csermely, P.1    Ágoston, V.2    Pongor, S.3
  • 10
    • 85018936850 scopus 로고    scopus 로고
    • Natural products sources and their active compounds on disease prevention: a Review
    • Jabeen, S., Hanif, M.A., Khan, M.M., Qadri, R.W.K., Natural products sources and their active compounds on disease prevention: a Review. IJCBS. 6 (2014), 76–83.
    • (2014) IJCBS. , vol.6 , pp. 76-83
    • Jabeen, S.1    Hanif, M.A.2    Khan, M.M.3    Qadri, R.W.K.4
  • 11
    • 85010767422 scopus 로고    scopus 로고
    • A novel bioconversion for value-added products from food waste using Musca domestica
    • Niu, Y., Zheng, D., Yao, B., Cai, Z., Zhao, Z., Wu, S., Cong, P., Yang, D., A novel bioconversion for value-added products from food waste using Musca domestica. Waste Manag. 61 (2017), 455–460, 10.1016/j.wasman.2016.10.054.
    • (2017) Waste Manag. , vol.61 , pp. 455-460
    • Niu, Y.1    Zheng, D.2    Yao, B.3    Cai, Z.4    Zhao, Z.5    Wu, S.6    Cong, P.7    Yang, D.8
  • 12
    • 84903853228 scopus 로고    scopus 로고
    • Sustainability of plant-based diets: back to the future
    • Sabaté, J., Soret, S., Sustainability of plant-based diets: back to the future. Am J. Clin. Nutr., 2014, 10.3945/ajcn.113.071522.
    • (2014) Am J. Clin. Nutr.
    • Sabaté, J.1    Soret, S.2
  • 13
    • 84874053136 scopus 로고    scopus 로고
    • A full-scale house fly (Diptera: Muscidae) larvae bioconversion system for value-added swine manure reduction
    • Wang, H., Zhang, Z., Czapar, G.F., Winkler, M.K.H., Zheng, J., A full-scale house fly (Diptera: Muscidae) larvae bioconversion system for value-added swine manure reduction. Waste Manag. Res. 31 (2013), 223–231, 10.1177/0734242x12469431.
    • (2013) Waste Manag. Res. , vol.31 , pp. 223-231
    • Wang, H.1    Zhang, Z.2    Czapar, G.F.3    Winkler, M.K.H.4    Zheng, J.5
  • 14
    • 81855183242 scopus 로고    scopus 로고
    • Energy-efficient food production to reduce global warming and ecodegradation: the use of edible insects
    • Premalatha, M., Abbasi, T., Abbasi, T., Abbasi, S.A., Energy-efficient food production to reduce global warming and ecodegradation: the use of edible insects. Renew. Sustain. Energy Rev. 15 (2011), 4357–4360, 10.1016/j.rser.2011.07.115.
    • (2011) Renew. Sustain. Energy Rev. , vol.15 , pp. 4357-4360
    • Premalatha, M.1    Abbasi, T.2    Abbasi, T.3    Abbasi, S.A.4
  • 15
    • 34047113472 scopus 로고    scopus 로고
    • Antibacterial activity and in vitro anti-tumor activity of the extract of the larvae of the housefly (Musca domestica)
    • Hou, L., Shi, Y., Zhai, P., Le, G., Antibacterial activity and in vitro anti-tumor activity of the extract of the larvae of the housefly (Musca domestica). J. Ethnopharmacol. 111 (2007), 227–231, 10.1016/j.jep.2006.11.015.
    • (2007) J. Ethnopharmacol. , vol.111 , pp. 227-231
    • Hou, L.1    Shi, Y.2    Zhai, P.3    Le, G.4
  • 16
    • 84893213181 scopus 로고    scopus 로고
    • Nutritional evaluation of dried larvae and pupae meal of the housefly (Musca domestica) using chemical-and broiler-based biological assays
    • Pieterse, E., Pretorius, Q., Nutritional evaluation of dried larvae and pupae meal of the housefly (Musca domestica) using chemical-and broiler-based biological assays. Anim. Prod. Sci. 54 (2014), 347–355, 10.1071/AN12370.
    • (2014) Anim. Prod. Sci. , vol.54 , pp. 347-355
    • Pieterse, E.1    Pretorius, Q.2
  • 17
    • 84987944961 scopus 로고    scopus 로고
    • Antioxidant activities of protein hydrolysates obtained from the housefly larvae
    • Zhang, H., Wang, P., Zhang, A.J., Li, X., Zhang, J.H., Qin, Q.L., et al. Antioxidant activities of protein hydrolysates obtained from the housefly larvae. Acta Biol. Hung. 67 (2016), 236–246, 10.1556/018.67.2016.3.2.
    • (2016) Acta Biol. Hung. , vol.67 , pp. 236-246
    • Zhang, H.1    Wang, P.2    Zhang, A.J.3    Li, X.4    Zhang, J.H.5    Qin, Q.L.6
  • 18
    • 84900319074 scopus 로고    scopus 로고
    • Anti-tumor and immunomodulatory activity of peptide fraction from the larvae of Musca domestica
    • Sun, H.X., Chen, L.Q., Zhang, J., Chen, F.Y., Anti-tumor and immunomodulatory activity of peptide fraction from the larvae of Musca domestica. J. Ethnopharmacol. 153 (2014), 831–839, 10.1016/j.jep.2014.03.052.
    • (2014) J. Ethnopharmacol. , vol.153 , pp. 831-839
    • Sun, H.X.1    Chen, L.Q.2    Zhang, J.3    Chen, F.Y.4
  • 19
    • 84355166473 scopus 로고    scopus 로고
    • Antioxidant, antifungal and antiviral activities of chitosan from the larvae of housefly, Musca domestica L
    • Ai, H., Wang, F., Xia, Y., Chen, X., Lei, C., Antioxidant, antifungal and antiviral activities of chitosan from the larvae of housefly, Musca domestica L. Food Chem. 132 (2012), 493–498, 10.1016/j.foodchem.2011.11.033.
    • (2012) Food Chem. , vol.132 , pp. 493-498
    • Ai, H.1    Wang, F.2    Xia, Y.3    Chen, X.4    Lei, C.5
  • 20
    • 85030253048 scopus 로고    scopus 로고
    • The Decoction
    • (Accessed 17 June 2017)
    • The Decoction. 2011 http://www2.lian.ch/downloads/Decotion_tipps_-_Raw_Herbs.pdf, (Accessed 17 June 2017).
    • (2011)
  • 21
    • 84897599642 scopus 로고    scopus 로고
    • Antioxidative activity of protein hydrolysate produced by alcalase hydrolysis from shrimp waste (Penaeus monodon and Penaeus indicus)
    • Dey, S.S., Dora, K.C., Antioxidative activity of protein hydrolysate produced by alcalase hydrolysis from shrimp waste (Penaeus monodon and Penaeus indicus). J. Food Sci. Technol. 51 (2014), 449–457, 10.1007/s13197-011-0512-z.
    • (2014) J. Food Sci. Technol. , vol.51 , pp. 449-457
    • Dey, S.S.1    Dora, K.C.2
  • 22
    • 27744513949 scopus 로고    scopus 로고
    • Effectiveness of fluorogenic substrates for angiotensin converting enzyme
    • Ando, S., Tamai, S., Nishikawa, H., Effectiveness of fluorogenic substrates for angiotensin converting enzyme. Pept. Sci. 2004 (2003), 343–346 http://ci.nii.ac.jp/naid/10012654362/.
    • (2003) Pept. Sci. , vol.2004 , pp. 343-346
    • Ando, S.1    Tamai, S.2    Nishikawa, H.3
  • 23
    • 85030223784 scopus 로고    scopus 로고
    • Application of angiotensin-Converting enzyme (ACE) assay with a fluorogenic substrate to the clinical chemistry
    • Ando, S., Matsubara, K., Zhang, B., Saku, K., Watanabe, L.A., Watanabe, H., Aoyagi, H., Application of angiotensin-Converting enzyme (ACE) assay with a fluorogenic substrate to the clinical chemistry. Pept. Sci. 2009 (2008), 341–344 http://ci.nii.ac.jp/naid/10027166481/.
    • (2008) Pept. Sci. , vol.2009 , pp. 341-344
    • Ando, S.1    Matsubara, K.2    Zhang, B.3    Saku, K.4    Watanabe, L.A.5    Watanabe, H.6    Aoyagi, H.7
  • 25
    • 84884510206 scopus 로고    scopus 로고
    • Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis
    • Nongonierma, A.B., Fitzgerald, R.J., Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis. Food Chem. 145 (2014), 845–852, 10.1016/j.foodchem.2013.08.097.
    • (2014) Food Chem. , vol.145 , pp. 845-852
    • Nongonierma, A.B.1    Fitzgerald, R.J.2
  • 26
    • 84937721348 scopus 로고    scopus 로고
    • Anti-α-glucosidase and anti-dipeptidyl peptidase-IV activities of extracts and purified compounds from Vitis thunbergii var taiwaniana
    • Lin, Y.S., Chen, C.R., Wu, W.H., Wen, C.L., Chang, C.I., Hou, W.C., Anti-α-glucosidase and anti-dipeptidyl peptidase-IV activities of extracts and purified compounds from Vitis thunbergii var taiwaniana. J. Agric. Food Chem. 63 (2015), 6393–6401, 10.1021/acs.jafc.5b02069.
    • (2015) J. Agric. Food Chem. , vol.63 , pp. 6393-6401
    • Lin, Y.S.1    Chen, C.R.2    Wu, W.H.3    Wen, C.L.4    Chang, C.I.5    Hou, W.C.6
  • 28
    • 0004032231 scopus 로고
    • Fao, Amino-acid Content of Foods and Biological Data On Proteins
    • (Accessed 20 June 2017)
    • Fao, Amino-acid Content of Foods and Biological Data On Proteins. 1981 http://www.fao.org/docrep/005/AC854T/AC854T46.htm, (Accessed 20 June 2017).
    • (1981)
  • 29
    • 0003526098 scopus 로고
    • FAO and WHO, Energy and Protein Requirements: Report of a Joint FAO/WHO Ad Hoc Expert Committee
    • (Accessed 17 June 2017)
    • FAO and WHO, Energy and Protein Requirements: Report of a Joint FAO/WHO Ad Hoc Expert Committee., 1973 http://apps.who.int/iris/bitstream/10665/41042/1/WHO_TRS_522_eng.pdf, (Accessed 17 June 2017).
    • (1973)
  • 30
    • 85030266073 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-iv inhibitor, patentWO2013125622 A1, (29 August). (Accessed 19 June 2017).
    • A. Yamada, D. Ochi, T. Sakurai, Dipeptidyl peptidase-iv inhibitor, patent WO2013125622 A1, (29 August, 2013). http://www.google.co.in/patents/WO2013125622A1?cl=en, (Accessed 19 June 2017).
    • (2013)
    • Yamada, A.1    Ochi, D.2    Sakurai, T.3
  • 31
    • 0032782991 scopus 로고    scopus 로고
    • Insects and other arthropods used as drugs in Korean traditional medicine
    • Pemberton, R.W., Insects and other arthropods used as drugs in Korean traditional medicine. J. Ethnopharmacol. 65 (1999), 207–216, 10.1016/S0378-8741(98)00209-8.
    • (1999) J. Ethnopharmacol. , vol.65 , pp. 207-216
    • Pemberton, R.W.1
  • 32
    • 84883590353 scopus 로고    scopus 로고
    • FAO, Edible Insects: Future Prospects for Food and Feed Security
    • (Accessed 11 May 2017)
    • FAO, Edible Insects: Future Prospects for Food and Feed Security. 2013 http://www.fao.org/docrep/018/i3253e/i3253e.pdf, (Accessed 11 May 2017).
    • (2013)
  • 33
    • 0035118090 scopus 로고    scopus 로고
    • Plasma lactate, GH and GH-binding protein levels in exercise following BCAA supplementation in athletes
    • De Palo, E.F., Gatti, R., Cappellin, E., Schiraldi, C., De Palo, C.B., Spinella, P., Plasma lactate, GH and GH-binding protein levels in exercise following BCAA supplementation in athletes. Amino Acids 20 (2001), 1–11, 10.1007/s007260170061.
    • (2001) Amino Acids , vol.20 , pp. 1-11
    • De Palo, E.F.1    Gatti, R.2    Cappellin, E.3    Schiraldi, C.4    De Palo, C.B.5    Spinella, P.6
  • 34
    • 85013156449 scopus 로고    scopus 로고
    • Influence of amino acids in dairy products on glucose homeostasis: the clinical evidence
    • Chartrand, D., Da Silva, M.S., Julien, P., Rudkowska, I., Influence of amino acids in dairy products on glucose homeostasis: the clinical evidence. Can. J. Diabetes 41 (2017), 329–337, 10.1016/j.jcjd.2016.10.009.
    • (2017) Can. J. Diabetes , vol.41 , pp. 329-337
    • Chartrand, D.1    Da Silva, M.S.2    Julien, P.3    Rudkowska, I.4
  • 35
    • 85000869948 scopus 로고    scopus 로고
    • The structure-Activity relationship of the antioxidant peptides from natural proteins
    • Zou, T.B., He, T.P., Li, H.B., Tang, H.W., Xia, E.Q., The structure-Activity relationship of the antioxidant peptides from natural proteins. Molecules, 21, 2016, 10.3390/molecules21010072.
    • (2016) Molecules , vol.21
    • Zou, T.B.1    He, T.P.2    Li, H.B.3    Tang, H.W.4    Xia, E.Q.5
  • 36
    • 84982162235 scopus 로고    scopus 로고
    • Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review
    • Nongonierma, A.B., FitzGerald, R.J., Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review. RSC Adv. 6 (2016), 75400–75413, 10.1039/C6RA12738J.
    • (2016) RSC Adv. , vol.6 , pp. 75400-75413
    • Nongonierma, A.B.1    FitzGerald, R.J.2
  • 37
    • 84861574479 scopus 로고    scopus 로고
    • Antioxidant activity and phenolic compounds of Holotrichia parallela Motschulsky extracts
    • Liu, S., Sun, J., Yu, L., Zhang, C., Bi, J., Zhu, F., Qu, M., Yang, Q., Antioxidant activity and phenolic compounds of Holotrichia parallela Motschulsky extracts. Food Chem. 134 (2012), 1885–1891, 10.1016/j.foodchem.2012.03.091.
    • (2012) Food Chem. , vol.134 , pp. 1885-1891
    • Liu, S.1    Sun, J.2    Yu, L.3    Zhang, C.4    Bi, J.5    Zhu, F.6    Qu, M.7    Yang, Q.8
  • 38
    • 80755126523 scopus 로고    scopus 로고
    • The effect of enzymes and hydrolysis conditions on degree of hydrolysis and DPPH radical scavenging activity of whey protein hydrolysates
    • Kamau, S.M., Lu, R.R., The effect of enzymes and hydrolysis conditions on degree of hydrolysis and DPPH radical scavenging activity of whey protein hydrolysates. Curr. Res. Dairy Sci. 3 (2011), 25–35, 10.3923/crds.2011.25.35.
    • (2011) Curr. Res. Dairy Sci. , vol.3 , pp. 25-35
    • Kamau, S.M.1    Lu, R.R.2
  • 39
    • 84864016547 scopus 로고    scopus 로고
    • Antioxidant, ace inhibitory activities and functional properties of egg white protein hydrolysate
    • Chen, C., Chi, Y.J., Antioxidant, ace inhibitory activities and functional properties of egg white protein hydrolysate. J. Food Biochem. 36 (2012), 383–394, 10.1111/j.1745-4514.2011.00555.x.
    • (2012) J. Food Biochem. , vol.36 , pp. 383-394
    • Chen, C.1    Chi, Y.J.2
  • 40
    • 84858997399 scopus 로고    scopus 로고
    • In vitro antioxidant activity of enzymatic hydrolysates prepared from abalone (Haliotis discus hannai Ino) viscera
    • Zhou, D.Y., Zhu, B.W., Qiao, L., Wu, H.T., Li, D.M., Yang, J.F., Murata, Y., In vitro antioxidant activity of enzymatic hydrolysates prepared from abalone (Haliotis discus hannai Ino) viscera. Food Bioprod. Process. 90 (2012), 148–154, 10.1016/j.fbp.2011.02.002.
    • (2012) Food Bioprod. Process. , vol.90 , pp. 148-154
    • Zhou, D.Y.1    Zhu, B.W.2    Qiao, L.3    Wu, H.T.4    Li, D.M.5    Yang, J.F.6    Murata, Y.7
  • 41
    • 84930649346 scopus 로고    scopus 로고
    • Influence of amino acid compositions and peptide profiles on antioxidant capacities of two protein hydrolysates from skipjack tuna (Katsuwonus pelamis) dark muscle
    • Chi, C.F., Hu, F.Y., Wang, B., Li, Z.R., Luo, H.Y., Influence of amino acid compositions and peptide profiles on antioxidant capacities of two protein hydrolysates from skipjack tuna (Katsuwonus pelamis) dark muscle. Mar. Drugs 13 (2015), 2580–2601, 10.3390/md13052580.
    • (2015) Mar. Drugs , vol.13 , pp. 2580-2601
    • Chi, C.F.1    Hu, F.Y.2    Wang, B.3    Li, Z.R.4    Luo, H.Y.5
  • 42
    • 22244448044 scopus 로고    scopus 로고
    • ACE inhibitory activity in enzymatic hydrolysates of insect protein
    • Vercruysse, L., Smagghe, G., Herregods, G., Van Camp, J., ACE inhibitory activity in enzymatic hydrolysates of insect protein. J. Agric. Food Chem. 53 (2005), 5207–5211, 10.1021/jf050337q.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 5207-5211
    • Vercruysse, L.1    Smagghe, G.2    Herregods, G.3    Van Camp, J.4
  • 43
    • 33749253681 scopus 로고    scopus 로고
    • The inhibitory effects of freshwater clam (Corbicula fluminea, Muller) muscle protein hydrolysates on angiotensin I converting enzyme
    • Tsai, J.S., Lin, T.C., Chen, J.L., Pan, B.S., The inhibitory effects of freshwater clam (Corbicula fluminea, Muller) muscle protein hydrolysates on angiotensin I converting enzyme. Process Biochem. 41 (2006), 2276–2281, 10.1016/j.procbio.2006.05.023.
    • (2006) Process Biochem. , vol.41 , pp. 2276-2281
    • Tsai, J.S.1    Lin, T.C.2    Chen, J.L.3    Pan, B.S.4
  • 44
    • 84868514774 scopus 로고    scopus 로고
    • Modeling the QSAR of ACE-inhibitory peptides with ANN and its applied illustration
    • He, R., Ma, H., Zhao, W., Qu, W., Zhao, J., Luo, L., Zhu, W., Modeling the QSAR of ACE-inhibitory peptides with ANN and its applied illustration. Int. J. Pept., 2012, 2012, 10.1155/2012/620609.
    • (2012) Int. J. Pept. , vol.2012
    • He, R.1    Ma, H.2    Zhao, W.3    Qu, W.4    Zhao, J.5    Luo, L.6    Zhu, W.7
  • 45
    • 84891647698 scopus 로고    scopus 로고
    • In vitro α-glucosidase, angiotensin converting enzyme and dipeptidyl peptidase-IV inhibitory properties of brewers’ spent grain protein hydrolysates
    • Connolly, A., Piggott, C.O., FitzGerald, R.J., In vitro α-glucosidase, angiotensin converting enzyme and dipeptidyl peptidase-IV inhibitory properties of brewers’ spent grain protein hydrolysates. Food Res. Int. 56 (2014), 100–107, 10.1016/j.foodres.2013.12.021.
    • (2014) Food Res. Int. , vol.56 , pp. 100-107
    • Connolly, A.1    Piggott, C.O.2    FitzGerald, R.J.3
  • 46
    • 84856555742 scopus 로고    scopus 로고
    • Peptides derived from Atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors
    • Li-Chan, E.C.Y., Hunag, S.L., Jao, C.L., Ho, K.P., Hsu, K.C., Peptides derived from Atlantic salmon skin gelatin as dipeptidyl-peptidase IV inhibitors. J. Agric. Food Chem. 60 (2012), 973–978, 10.1021/jf204720q.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 973-978
    • Li-Chan, E.C.Y.1    Hunag, S.L.2    Jao, C.L.3    Ho, K.P.4    Hsu, K.C.5
  • 47
    • 84887176534 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitory peptides generated in Spanish dry-cured ham
    • Gallego, M., Aristoy, M.C., Toldrá, F., Dipeptidyl peptidase IV inhibitory peptides generated in Spanish dry-cured ham. Meat Sci. 96 (2014), 757–761, 10.1016/j.meatsci.2013.09.014.
    • (2014) Meat Sci. , vol.96 , pp. 757-761
    • Gallego, M.1    Aristoy, M.C.2    Toldrá, F.3
  • 48
    • 85018661360 scopus 로고    scopus 로고
    • Marine peptides as potential agents for the management of type 2 diabetes Mellitus—A prospect
    • Xia, E.Q., Zhu, S.S., He, M.J., Luo, F., Fu, C.Z., Zou, T.B., Marine peptides as potential agents for the management of type 2 diabetes Mellitus—A prospect. Mar. Drugs, 15, 2017, 88, 10.3390/md15040088.
    • (2017) Mar. Drugs , vol.15 , pp. 88
    • Xia, E.Q.1    Zhu, S.S.2    He, M.J.3    Luo, F.4    Fu, C.Z.5    Zou, T.B.6
  • 50
    • 84930182439 scopus 로고    scopus 로고
    • The evaluation of dipeptidyl peptidase (DPP)-IV, α-Glucosidase and angiotensin converting enzyme (ACE) inhibitory activities of whey proteins hydrolyzed with serine protease isolated from asian pumpkin (Cucurbita ficifolia)
    • Konrad, B., Anna, D., Marek, S., Marta, P., Aleksandra, Z., Józefa, C., The evaluation of dipeptidyl peptidase (DPP)-IV, α-Glucosidase and angiotensin converting enzyme (ACE) inhibitory activities of whey proteins hydrolyzed with serine protease isolated from asian pumpkin (Cucurbita ficifolia). Int. J. Pept. Res. Ther. 20 (2014), 483–491, 10.1007/s10989-014-9413-0.
    • (2014) Int. J. Pept. Res. Ther. , vol.20 , pp. 483-491
    • Konrad, B.1    Anna, D.2    Marek, S.3    Marta, P.4    Aleksandra, Z.5    Józefa, C.6
  • 51
    • 84865746765 scopus 로고    scopus 로고
    • ACE inhibitory peptides and antioxidant peptides derived from in vitro digestion hydrolysate of hen egg white lysozyme
    • Rao, S., Sun, J., Liu, Y., Zeng, H., Su, Y., Yang, Y., ACE inhibitory peptides and antioxidant peptides derived from in vitro digestion hydrolysate of hen egg white lysozyme. Food Chem. 135 (2012), 1245–1252, 10.1016/j.foodchem.2012.05.059.
    • (2012) Food Chem. , vol.135 , pp. 1245-1252
    • Rao, S.1    Sun, J.2    Liu, Y.3    Zeng, H.4    Su, Y.5    Yang, Y.6
  • 52
    • 80052590329 scopus 로고    scopus 로고
    • Functional amino acids in growth, reproduction, and health
    • Wu, G., Functional amino acids in growth, reproduction, and health. Adv. Nutr. 1 (2010), 31–37, 10.3945/an.110.1008.
    • (2010) Adv. Nutr. , vol.1 , pp. 31-37
    • Wu, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.