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Volumn 1401, Issue 1, 2017, Pages 28-36

Plant non-starch polysaccharides that inhibit key enzymes linked to type 2 diabetes mellitus

Author keywords

inhibition activity; key enzymes; plant non starch polysaccharides; type 2 diabetes mellitus

Indexed keywords

ALPHA GLUCOSIDASE; AMYLASE; DIPEPTIDYL PEPTIDASE IV; ENZYME; POLYSACCHARIDE; TRIACYLGLYCEROL LIPASE; ENZYME INHIBITOR; PLANT EXTRACT;

EID: 85030615159     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/nyas.13430     Document Type: Review
Times cited : (41)

References (66)
  • 1
    • 84962307139 scopus 로고    scopus 로고
    • Mechanisms underlying the effect of polysaccharides in the treatment of type 2 diabetes: a review
    • Wu, J., S. Shi, H. Wang, et al. 2016. Mechanisms underlying the effect of polysaccharides in the treatment of type 2 diabetes: a review. Carbohydr. Polym. 144: 474–494.
    • (2016) Carbohydr. Polym. , vol.144 , pp. 474-494
    • Wu, J.1    Shi, S.2    Wang, H.3
  • 2
    • 84964579589 scopus 로고    scopus 로고
    • Anti-diabetic polysaccharides from natural sources: a review
    • Wang, P.-C., S. Zhao, B.-Y. Yang, et al. 2016. Anti-diabetic polysaccharides from natural sources: a review. Carbohydr. Polym. 148: 86–97.
    • (2016) Carbohydr. Polym. , vol.148 , pp. 86-97
    • Wang, P.-C.1    Zhao, S.2    Yang, B.-Y.3
  • 3
    • 84862119222 scopus 로고    scopus 로고
    • European guidelines on cardiovascular disease prevention in clinical practice (version 2012)
    • Perk, J., G. De Backer, H. Gohlke, et al. 2012. European guidelines on cardiovascular disease prevention in clinical practice (version 2012). Eur. Heart J. 33: 1635–1701.
    • (2012) Eur. Heart J. , vol.33 , pp. 1635-1701
    • Perk, J.1    De Backer, G.2    Gohlke, H.3
  • 4
    • 83955163773 scopus 로고    scopus 로고
    • Anti-diabetic activities of phenolic compounds in muscadine against alpha-glucosidase and pancreatic lipase
    • You, Q., F. Chen, X. Wang, et al. 2012. Anti-diabetic activities of phenolic compounds in muscadine against alpha-glucosidase and pancreatic lipase. LWT – Food Sci. Technol. 46: 164–168.
    • (2012) LWT – Food Sci. Technol. , vol.46 , pp. 164-168
    • You, Q.1    Chen, F.2    Wang, X.3
  • 5
    • 33845881411 scopus 로고    scopus 로고
    • Mechanisms linking obesity to insulin resistance and type 2 diabetes
    • Kahn, S.E., R.L. Hull & K.M. Utzschneider. 2006. Mechanisms linking obesity to insulin resistance and type 2 diabetes. Nature 444: 840–846.
    • (2006) Nature , vol.444 , pp. 840-846
    • Kahn, S.E.1    Hull, R.L.2    Utzschneider, K.M.3
  • 6
    • 84871166499 scopus 로고    scopus 로고
    • GLP-1 receptor activated insulin secretion from pancreatic β-cells: mechanism and glucose dependence
    • Meloni, A.R., M.B. DeYoung, C. Lowe, et al. 2013. GLP-1 receptor activated insulin secretion from pancreatic β-cells: mechanism and glucose dependence. Diabetes Obes. Metab. 15: 15–27.
    • (2013) Diabetes Obes. Metab. , vol.15 , pp. 15-27
    • Meloni, A.R.1    DeYoung, M.B.2    Lowe, C.3
  • 7
    • 33846616718 scopus 로고    scopus 로고
    • Hypoglycemia-induced myocardial infarction: an unusual adverse effect of sulfonylureas
    • Chang, J.-H., C.-F. Tseng & J.-Y. Wang. 2007. Hypoglycemia-induced myocardial infarction: an unusual adverse effect of sulfonylureas. Int. J. Cardiol. 115: 414–416.
    • (2007) Int. J. Cardiol. , vol.115 , pp. 414-416
    • Chang, J.-H.1    Tseng, C.-F.2    Wang, J.-Y.3
  • 8
    • 34247519288 scopus 로고    scopus 로고
    • Review article: drug hepatotoxicity
    • Chang, C. & T. Schiano. 2007. Review article: drug hepatotoxicity. Aliment. Pharmacol. Ther. 25: 1135–1151.
    • (2007) Aliment. Pharmacol. Ther. , vol.25 , pp. 1135-1151
    • Chang, C.1    Schiano, T.2
  • 9
    • 11844294865 scopus 로고    scopus 로고
    • α-Glucosidase inhibitors for patients with type 2 diabetes: results from a Cochrane systematic review and meta-analysis
    • Van De Laar, F.A., P.L. Lucassen, R.P. Akkermans, et al. 2005. α-Glucosidase inhibitors for patients with type 2 diabetes: results from a Cochrane systematic review and meta-analysis. Diabetes Care 28: 154–163.
    • (2005) Diabetes Care , vol.28 , pp. 154-163
    • Van De Laar, F.A.1    Lucassen, P.L.2    Akkermans, R.P.3
  • 10
    • 2642580716 scopus 로고    scopus 로고
    • Mortality in type 2 diabetic subjects prescribed metformin and sulphonylurea drugs in combination: cohort study
    • Gulliford, M. & R. Latinovic. 2004. Mortality in type 2 diabetic subjects prescribed metformin and sulphonylurea drugs in combination: cohort study. Diabetes Metab. Res. Rev. 20: 239–245.
    • (2004) Diabetes Metab. Res. Rev. , vol.20 , pp. 239-245
    • Gulliford, M.1    Latinovic, R.2
  • 11
    • 84863548364 scopus 로고    scopus 로고
    • Dietary roles of non-starch polysachharides in human nutrition: a review
    • Kumar, V., A.K. Sinha, H.P.S. Makkar, et al. 2012. Dietary roles of non-starch polysachharides in human nutrition: a review. Crit. Rev. Food Sci. Nutr. 52: 899–935.
    • (2012) Crit. Rev. Food Sci. Nutr. , vol.52 , pp. 899-935
    • Kumar, V.1    Sinha, A.K.2    Makkar, H.P.S.3
  • 13
    • 0032054552 scopus 로고    scopus 로고
    • Fiber: forms and functions
    • Davidson, M.H. & A. McDonald. 1998. Fiber: forms and functions. Nutr. Res. 18: 617–624.
    • (1998) Nutr. Res. , vol.18 , pp. 617-624
    • Davidson, M.H.1    McDonald, A.2
  • 14
    • 84947612915 scopus 로고    scopus 로고
    • Effect of thermostable α-amylase addition on the physicochemical properties, free/bound phenolics and antioxidant capacities of extruded hulled and whole rice
    • Xu, E., Z. Wu, J. Long, et al. 2015. Effect of thermostable α-amylase addition on the physicochemical properties, free/bound phenolics and antioxidant capacities of extruded hulled and whole rice. Food Bioprocess Tech. 8: 1958–1973.
    • (2015) Food Bioprocess Tech , vol.8 , pp. 1958-1973
    • Xu, E.1    Wu, Z.2    Long, J.3
  • 15
    • 84877149580 scopus 로고    scopus 로고
    • Inhibitory activities of Ulva lactuca polysaccharides on digestive enzymes related to diabetes and obesity
    • BelHadj, S., O. Hentati, A. Elfeki, et al. 2013. Inhibitory activities of Ulva lactuca polysaccharides on digestive enzymes related to diabetes and obesity. Arch. Physiol. Biochem. 119: 81–87.
    • (2013) Arch. Physiol. Biochem. , vol.119 , pp. 81-87
    • BelHadj, S.1    Hentati, O.2    Elfeki, A.3
  • 16
    • 1942424088 scopus 로고    scopus 로고
    • Natural medicines used in the traditional Chinese medical system for therapy of diabetes mellitus
    • Li, W., H. Zheng, J. Bukuru, et al. 2004. Natural medicines used in the traditional Chinese medical system for therapy of diabetes mellitus. J. Ethnopharmacol. 92: 1–21.
    • (2004) J. Ethnopharmacol. , vol.92 , pp. 1-21
    • Li, W.1    Zheng, H.2    Bukuru, J.3
  • 17
    • 84907100427 scopus 로고    scopus 로고
    • Inhibition of α-glucosidase by polysaccharides from the fruit hull of Camellia oleifera Abel
    • Zhang, S. & X.-Z. Li. 2015. Inhibition of α-glucosidase by polysaccharides from the fruit hull of Camellia oleifera Abel. Carbohydr. Polym. 115: 38–43.
    • (2015) Carbohydr. Polym. , vol.115 , pp. 38-43
    • Zhang, S.1    Li, X.-Z.2
  • 18
    • 84959299122 scopus 로고    scopus 로고
    • Structural characterization, α-glucosidase inhibitory and DPPH scavenging activities of polysaccharides from guava
    • Zhang, Z., F. Kong, H. Ni, et al. 2016. Structural characterization, α-glucosidase inhibitory and DPPH scavenging activities of polysaccharides from guava. Carbohydr. Polym. 144: 106–114.
    • (2016) Carbohydr. Polym. , vol.144 , pp. 106-114
    • Zhang, Z.1    Kong, F.2    Ni, H.3
  • 19
    • 84879036118 scopus 로고    scopus 로고
    • The α-amylase and α-glucosidase inhibitory effects of Irish seaweed extracts
    • Lordan, S., T.J. Smyth, A. Soler-Vila, et al. 2013. The α-amylase and α-glucosidase inhibitory effects of Irish seaweed extracts. Food Chem. 141: 2170–2176.
    • (2013) Food Chem , vol.141 , pp. 2170-2176
    • Lordan, S.1    Smyth, T.J.2    Soler-Vila, A.3
  • 20
    • 0028933531 scopus 로고
    • Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution
    • Machius, M., G. Wiegand & R. Huber. 1995. Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. J. Mol. Biol. 246: 545–559.
    • (1995) J. Mol. Biol. , vol.246 , pp. 545-559
    • Machius, M.1    Wiegand, G.2    Huber, R.3
  • 21
    • 3042670288 scopus 로고    scopus 로고
    • An overview of the microbial α-amylase family
    • Reddy, N., A. Nimmagadda & K.S. Rao. 2003. An overview of the microbial α-amylase family. Afr. J. Biotechnol. 2: 645–648.
    • (2003) Afr. J. Biotechnol. , vol.2 , pp. 645-648
    • Reddy, N.1    Nimmagadda, A.2    Rao, K.S.3
  • 22
    • 33846865308 scopus 로고    scopus 로고
    • Inhibitory potential of herb, fruit, and fungal-enriched cheese against key enzymes linked to type 2 diabetes and hypertension
    • Apostolidis, E., Y.-I. Kwon & K. Shetty. 2007. Inhibitory potential of herb, fruit, and fungal-enriched cheese against key enzymes linked to type 2 diabetes and hypertension. Innov. Food Sci. Emerg. Technol. 8: 46–54.
    • (2007) Innov. Food Sci. Emerg. Technol. , vol.8 , pp. 46-54
    • Apostolidis, E.1    Kwon, Y.-I.2    Shetty, K.3
  • 23
    • 78650290984 scopus 로고    scopus 로고
    • In vitro antioxidant and inhibitory potential of Terminalia bellerica and Emblica officinalis fruits against LDL oxidation and key enzymes linked to type 2 diabetes
    • Nampoothiri, S.V., A. Prathapan, O.L. Cherian, et al. 2011. In vitro antioxidant and inhibitory potential of Terminalia bellerica and Emblica officinalis fruits against LDL oxidation and key enzymes linked to type 2 diabetes. Food Chem. Toxicol. 49: 125–131.
    • (2011) Food Chem. Toxicol. , vol.49 , pp. 125-131
    • Nampoothiri, S.V.1    Prathapan, A.2    Cherian, O.L.3
  • 24
    • 84880182665 scopus 로고    scopus 로고
    • Chemical modification, antioxidant and α-amylase inhibitory activities of corn silk polysaccharides
    • Chen, S., H. Chen, J. Tian, et al. 2013. Chemical modification, antioxidant and α-amylase inhibitory activities of corn silk polysaccharides. Carbohydr. Polym. 98: 428–437.
    • (2013) Carbohydr. Polym. , vol.98 , pp. 428-437
    • Chen, S.1    Chen, H.2    Tian, J.3
  • 25
    • 84929626550 scopus 로고    scopus 로고
    • Optimization for ultrasound extraction of polysaccharides from mulberry fruits with antioxidant and hyperglycemic activity in vitro
    • Chen, C., L.-J. You, A.M. Abbasi, et al. 2015. Optimization for ultrasound extraction of polysaccharides from mulberry fruits with antioxidant and hyperglycemic activity in vitro. Carbohydr. Polym. 130: 122–132.
    • (2015) Carbohydr. Polym. , vol.130 , pp. 122-132
    • Chen, C.1    You, L.-J.2    Abbasi, A.M.3
  • 26
    • 84922774666 scopus 로고    scopus 로고
    • Inhibition of α-amylase activity by cellulose: kinetic analysis and nutritional implications
    • Dhital, S., M.J. Gidley & F.J. Warren. 2015. Inhibition of α-amylase activity by cellulose: kinetic analysis and nutritional implications. Carbohydr. Polym. 123: 305–312.
    • (2015) Carbohydr. Polym. , vol.123 , pp. 305-312
    • Dhital, S.1    Gidley, M.J.2    Warren, F.J.3
  • 27
    • 84872477076 scopus 로고    scopus 로고
    • In vitro effects of a novel polysaccharide from the seeds of Plantago asiatica L. on intestinal function
    • Hu, J.-L., S.-P. Nie, C. Li, et al. 2013. In vitro effects of a novel polysaccharide from the seeds of Plantago asiatica L. on intestinal function. Int. J. Biol. Macromol. 54: 264–269.
    • (2013) Int. J. Biol. Macromol. , vol.54 , pp. 264-269
    • Hu, J.-L.1    Nie, S.-P.2    Li, C.3
  • 28
    • 84866526769 scopus 로고    scopus 로고
    • Chemical composition and bioactivities of a water-soluble polysaccharide from the endodermis of shaddock
    • Liu, G., S. Xu & L. Chen. 2012. Chemical composition and bioactivities of a water-soluble polysaccharide from the endodermis of shaddock. Int. J. Biol. Macromol. 51: 763–766.
    • (2012) Int. J. Biol. Macromol. , vol.51 , pp. 763-766
    • Liu, G.1    Xu, S.2    Chen, L.3
  • 29
    • 84908610688 scopus 로고    scopus 로고
    • Fucoidan–A α-d-glucosidase inhibitor from Sargassum wightii with relevance to type 2 diabetes mellitus therapy
    • Kumar, T.V., S. Lakshmanasenthil, D. Geetharamani, et al. 2015. Fucoidan–A α-d-glucosidase inhibitor from Sargassum wightii with relevance to type 2 diabetes mellitus therapy. Int. J. Biol. Macromol. 72: 1044–1047.
    • (2015) Int. J. Biol. Macromol. , vol.72 , pp. 1044-1047
    • Kumar, T.V.1    Lakshmanasenthil, S.2    Geetharamani, D.3
  • 31
    • 84943819587 scopus 로고    scopus 로고
    • Molecular weight and sulfate content modulate the inhibition of α-amylase by fucoidan relevant for type 2 diabetes management
    • Kim, K.-T., L.-E. Rioux & S.L. Turgeon. 2015. Molecular weight and sulfate content modulate the inhibition of α-amylase by fucoidan relevant for type 2 diabetes management. PharmaNutrition 3: 108–114.
    • (2015) PharmaNutrition , vol.3 , pp. 108-114
    • Kim, K.-T.1    Rioux, L.-E.2    Turgeon, S.L.3
  • 32
    • 84861580431 scopus 로고    scopus 로고
    • Composition, characteristics, and in-vitro physiological effects of the water-soluble polysaccharides from Cassia seed
    • Huang, Y.-L., C.-J. Chow & Y.-H. Tsai. 2012. Composition, characteristics, and in-vitro physiological effects of the water-soluble polysaccharides from Cassia seed. Food Chem. 134: 1967–1972.
    • (2012) Food Chem , vol.134 , pp. 1967-1972
    • Huang, Y.-L.1    Chow, C.-J.2    Tsai, Y.-H.3
  • 33
    • 0034491587 scopus 로고    scopus 로고
    • Phytate and phytase: consequences for protein utilisation
    • Selle, P., V. Ravindran, A. Caldwell, et al. 2000. Phytate and phytase: consequences for protein utilisation. Nutr. Res. Rev. 13: 255–278.
    • (2000) Nutr. Res. Rev. , vol.13 , pp. 255-278
    • Selle, P.1    Ravindran, V.2    Caldwell, A.3
  • 34
    • 84858328042 scopus 로고    scopus 로고
    • Immobilization of B. amyloliquefaciens α-amylase and comparison of some of its enzymatic properties with the free form
    • Demirkan, E., S. Dincbas, N. Sevinc, et al. 2011. Immobilization of B. amyloliquefaciens α-amylase and comparison of some of its enzymatic properties with the free form. Rom. Biotechnol. Lett. 16: 6690–6701.
    • (2011) Rom. Biotechnol. Lett. , vol.16 , pp. 6690-6701
    • Demirkan, E.1    Dincbas, S.2    Sevinc, N.3
  • 35
    • 0035897508 scopus 로고    scopus 로고
    • Use of tannin-binding chemicals to assay for tannins and their negative postingestive effects in ruminants
    • Silanikove, N., A. Perevolotsky & F.D. Provenza. 2001. Use of tannin-binding chemicals to assay for tannins and their negative postingestive effects in ruminants. Anim. Feed Sci. Technol. 91: 69–81.
    • (2001) Anim. Feed Sci. Technol. , vol.91 , pp. 69-81
    • Silanikove, N.1    Perevolotsky, A.2    Provenza, F.D.3
  • 36
    • 0031201675 scopus 로고    scopus 로고
    • Molecular mechanism in α-glucosidase and glucoamylase
    • Chiba, S. 1997. Molecular mechanism in α-glucosidase and glucoamylase. Biosci. Biotechnol. Biochem. 61: 1233–1239.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1233-1239
    • Chiba, S.1
  • 37
    • 0025866164 scopus 로고
    • Human lysosomal alpha-glucosidase. Characterization of the catalytic site
    • Hermans, M., M. Kroos, J. Van Beeumen, et al. 1991. Human lysosomal alpha-glucosidase. Characterization of the catalytic site. J. Biol. Chem. 266: 13507–13512.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13507-13512
    • Hermans, M.1    Kroos, M.2    Van Beeumen, J.3
  • 38
    • 0016749864 scopus 로고
    • Carbohydrate digestion and absorption: role of the small intestine
    • Gray, G.M. 1975. Carbohydrate digestion and absorption: role of the small intestine. N. Engl. J. Med. 292: 1225–1230.
    • (1975) N. Engl. J. Med. , vol.292 , pp. 1225-1230
    • Gray, G.M.1
  • 39
    • 84872781682 scopus 로고    scopus 로고
    • Soybean phenolic-rich extracts inhibit key-enzymes linked to type 2 diabetes (α-amylase and α-glucosidase) and hypertension (angiotensin I converting enzyme) in vitro
    • Ademiluyi, A.O. & G. Oboh. 2013. Soybean phenolic-rich extracts inhibit key-enzymes linked to type 2 diabetes (α-amylase and α-glucosidase) and hypertension (angiotensin I converting enzyme) in vitro. Exp. Toxicol. Pathol. 65: 305–309.
    • (2013) Exp. Toxicol. Pathol. , vol.65 , pp. 305-309
    • Ademiluyi, A.O.1    Oboh, G.2
  • 40
    • 84892947782 scopus 로고    scopus 로고
    • Alpha-amylase and alpha-glucosidase inhibition is differentially modulated by fucoidan obtained from Fucus vesiculosus and Ascophyllum nodosum
    • Kim, K.-T., L.-E. Rioux & S.L. Turgeon. 2014. Alpha-amylase and alpha-glucosidase inhibition is differentially modulated by fucoidan obtained from Fucus vesiculosus and Ascophyllum nodosum. Phytochemistry 98: 27–33.
    • (2014) Phytochemistry , vol.98 , pp. 27-33
    • Kim, K.-T.1    Rioux, L.-E.2    Turgeon, S.L.3
  • 41
    • 84954154455 scopus 로고    scopus 로고
    • Antioxidation and α-glucosidase inhibitory activities of barley polysaccharides modified with sulfation
    • Qian, J.-Y., Y.-Y. Bai, J. Tang, et al. 2015. Antioxidation and α-glucosidase inhibitory activities of barley polysaccharides modified with sulfation. LWT – Food Sci. Technol. 64: 104–111.
    • (2015) LWT – Food Sci. Technol. , vol.64 , pp. 104-111
    • Qian, J.-Y.1    Bai, Y.-Y.2    Tang, J.3
  • 42
    • 78751702470 scopus 로고    scopus 로고
    • Inhibitory effects of fucan sulfates on enzymatic hydrolysis of starch
    • Cho, M., J.H. Han & S. You. 2011. Inhibitory effects of fucan sulfates on enzymatic hydrolysis of starch. LWT – Food Sci. Technol. 44: 1164–1171.
    • (2011) LWT – Food Sci. Technol. , vol.44 , pp. 1164-1171
    • Cho, M.1    Han, J.H.2    You, S.3
  • 43
    • 33748708627 scopus 로고    scopus 로고
    • α-and β-Glucosidase inhibitors: chemical structure and biological activity
    • De Melo, E.B., A. Gomes & I. Carvalho. 2006. α-and β-Glucosidase inhibitors: chemical structure and biological activity. Tetrahedron 62: 10277–10302.
    • (2006) Tetrahedron , vol.62 , pp. 10277-10302
    • De Melo, E.B.1    Gomes, A.2    Carvalho, I.3
  • 44
    • 0028860889 scopus 로고
    • Mechanism-based inhibition of yeast α-glucosidase and human pancreatic α-amylase by a new class of inhibitors 2-deoxy-2, 2-difluoro-α-glycosides
    • Braun, C., G.D. Brayer & S.G. Withers. 1995. Mechanism-based inhibition of yeast α-glucosidase and human pancreatic α-amylase by a new class of inhibitors 2-deoxy-2, 2-difluoro-α-glycosides. J. Biol. Chem. 270: 26778–26781.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26778-26781
    • Braun, C.1    Brayer, G.D.2    Withers, S.G.3
  • 45
    • 34447326170 scopus 로고    scopus 로고
    • Zwitterionic glycosidase inhibitors: salacinol and related analogues
    • Mohan, S. & B.M. Pinto. 2007. Zwitterionic glycosidase inhibitors: salacinol and related analogues. Carbohydr. Res. 342: 1551–1580.
    • (2007) Carbohydr. Res. , vol.342 , pp. 1551-1580
    • Mohan, S.1    Pinto, B.M.2
  • 47
    • 0025062291 scopus 로고
    • Structure of human pancreatic lipase
    • Winkler, F.K., A. D'Arcy & W. Hunziker. 1990. Structure of human pancreatic lipase. Nature 343: 771−774.
    • (1990) Nature , vol.343 , pp. 771-774
    • Winkler, F.K.1    D'Arcy, A.2    Hunziker, W.3
  • 48
    • 0036460675 scopus 로고    scopus 로고
    • Lipoprotein lipase: structure, function, regulation, and role in disease
    • Mead, J.R., S.A. Irvine & D.P. Ramji. 2002. Lipoprotein lipase: structure, function, regulation, and role in disease. J. Mol. Med. 80: 753–769.
    • (2002) J. Mol. Med. , vol.80 , pp. 753-769
    • Mead, J.R.1    Irvine, S.A.2    Ramji, D.P.3
  • 49
    • 0034300099 scopus 로고    scopus 로고
    • Activity and stability of lipase in AOT reversed micelles with bile salt cosurfactant
    • Freeman, K.S., T.T. Tang, R.D. Shah, et al. 2000. Activity and stability of lipase in AOT reversed micelles with bile salt cosurfactant. J. Phys. Chem. B 104: 9312–9316.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 9312-9316
    • Freeman, K.S.1    Tang, T.T.2    Shah, R.D.3
  • 50
    • 84884835984 scopus 로고    scopus 로고
    • A broader view: microbial enzymes and their relevance in industries, medicine, and beyond
    • Gurung, N., S. Ray, S. Bose, et al. 2013. A broader view: microbial enzymes and their relevance in industries, medicine, and beyond. Biomed. Res. Int. 2013: 1–18.
    • (2013) Biomed. Res. Int. , vol.2013 , pp. 1-18
    • Gurung, N.1    Ray, S.2    Bose, S.3
  • 51
    • 77951642395 scopus 로고    scopus 로고
    • Enzymatic synthesis of structured lipids using a novel cold-active lipase from Pichia lynferdii NRRL Y-7723
    • Kim, H.R., C.T. Hou, K.T. Lee, et al. 2010. Enzymatic synthesis of structured lipids using a novel cold-active lipase from Pichia lynferdii NRRL Y-7723. Food Chem. 122: 846–849.
    • (2010) Food Chem , vol.122 , pp. 846-849
    • Kim, H.R.1    Hou, C.T.2    Lee, K.T.3
  • 52
    • 33846880700 scopus 로고    scopus 로고
    • Inhibition of lipase activities by basic polysaccharide
    • Tsujita, T., H. Takaichi, T. Takaku, et al. 2007. Inhibition of lipase activities by basic polysaccharide. J. Lipid Res. 48: 358–365.
    • (2007) J. Lipid Res. , vol.48 , pp. 358-365
    • Tsujita, T.1    Takaichi, H.2    Takaku, T.3
  • 53
    • 84883654526 scopus 로고    scopus 로고
    • Inhibitory activities of three Malaysian edible seaweeds on lipase and α-amylase
    • Balasubramaniam, V., S. Mustar, N. Mustafa Khalid, et al. 2013. Inhibitory activities of three Malaysian edible seaweeds on lipase and α-amylase. J. Appl. Phycol. 25: 1405–1412.
    • (2013) J. Appl. Phycol. , vol.25 , pp. 1405-1412
    • Balasubramaniam, V.1    Mustar, S.2    Mustafa Khalid, N.3
  • 54
    • 0042131827 scopus 로고    scopus 로고
    • Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV
    • Thoma, R., B. Löffler, M. Stihle, et al. 2003. Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure 11: 947–959.
    • (2003) Structure , vol.11 , pp. 947-959
    • Thoma, R.1    Löffler, B.2    Stihle, M.3
  • 55
    • 0031932784 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV/CD26 on T cells: analysis of an alternative T-cell activation pathway
    • Bonin, A., J. Hühn & B. Fleischer. 1998. Dipeptidyl-peptidase IV/CD26 on T cells: analysis of an alternative T-cell activation pathway. Immunol. Rev. 161: 43–53.
    • (1998) Immunol. Rev. , vol.161 , pp. 43-53
    • Bonin, A.1    Hühn, J.2    Fleischer, B.3
  • 56
    • 0027473729 scopus 로고
    • Pancreatic beta-cells are rendered glucose-competent by the insulinotropic hormone glucagon-like peptide-1 (7–37)
    • Holz, G.G., W.M. Kühtreiber & J.F. Habener. 1993. Pancreatic beta-cells are rendered glucose-competent by the insulinotropic hormone glucagon-like peptide-1 (7–37). Nature 361: 362–365.
    • (1993) Nature , vol.361 , pp. 362-365
    • Holz, G.G.1    Kühtreiber, W.M.2    Habener, J.F.3
  • 57
    • 84870054636 scopus 로고    scopus 로고
    • GLP-1 receptor agonists for individualized treatment of type 2 diabetes mellitus
    • Meier, J.J. 2012. GLP-1 receptor agonists for individualized treatment of type 2 diabetes mellitus. Nat. Rev. Endocrinol. 8: 728–742.
    • (2012) Nat. Rev. Endocrinol. , vol.8 , pp. 728-742
    • Meier, J.J.1
  • 58
    • 78649686908 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitors in the treatment of type 2 diabetes: a comparative review
    • Deacon, C.F. 2011. Dipeptidyl peptidase-4 inhibitors in the treatment of type 2 diabetes: a comparative review. Diabetes Obes. Metab. 13: 7–18.
    • (2011) Diabetes Obes. Metab. , vol.13 , pp. 7-18
    • Deacon, C.F.1
  • 59
    • 1042268736 scopus 로고    scopus 로고
    • One-year glycemic control with a sulfonylurea plus pioglitazone versus a sulfonylurea plus metformin in patients with type 2 diabetes
    • Hanefeld, M., P. Brunetti, G.H. Schernthaner, et al. 2004. One-year glycemic control with a sulfonylurea plus pioglitazone versus a sulfonylurea plus metformin in patients with type 2 diabetes. Diabetes Care 27: 141–147.
    • (2004) Diabetes Care , vol.27 , pp. 141-147
    • Hanefeld, M.1    Brunetti, P.2    Schernthaner, G.H.3
  • 60
    • 4744373549 scopus 로고    scopus 로고
    • The hypoglycemic effects of hesperidin and naringin are partly mediated by hepatic glucose-regulating enzymes in C57BL/KsJ-db/db mice
    • Jung, U.J., M.-K. Lee, K.-S. Jeong, et al. 2004. The hypoglycemic effects of hesperidin and naringin are partly mediated by hepatic glucose-regulating enzymes in C57BL/KsJ-db/db mice. J. Nutr. 134: 2499–2503.
    • (2004) J. Nutr. , vol.134 , pp. 2499-2503
    • Jung, U.J.1    Lee, M.-K.2    Jeong, K.-S.3
  • 61
    • 0033548086 scopus 로고    scopus 로고
    • Truncation of macrophage-derived chemokine by CD26/dipeptidyl-peptidase IV beyond its predicted cleavage site affects chemotactic activity and CC chemokine receptor 4 interaction
    • Proost, P., S. Struyf, D. Schols, et al. 1999. Truncation of macrophage-derived chemokine by CD26/dipeptidyl-peptidase IV beyond its predicted cleavage site affects chemotactic activity and CC chemokine receptor 4 interaction. J. Biol. Chem. 274: 3988–3993.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3988-3993
    • Proost, P.1    Struyf, S.2    Schols, D.3
  • 62
    • 0034635440 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs
    • Hinke, S.A., J.A. Pospisilik, H.-U. Demuth, et al. 2000. Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs. J. Biol. Chem. 275: 3827–3834.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3827-3834
    • Hinke, S.A.1    Pospisilik, J.A.2    Demuth, H.-U.3
  • 63
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26)—role in the inactivation of regulatory peptides
    • Mentlein, R. 1999. Dipeptidyl-peptidase IV (CD26)—role in the inactivation of regulatory peptides. Regul. Pept. 85: 9–24.
    • (1999) Regul. Pept. , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 64
    • 48849097624 scopus 로고    scopus 로고
    • The search for novel human pancreatic α-amylase inhibitors: high-throughput screening of terrestrial and marine natural product extracts
    • Tarling, C.A., K. Woods, R. Zhang, et al. 2008. The search for novel human pancreatic α-amylase inhibitors: high-throughput screening of terrestrial and marine natural product extracts. ChemBioChem 9: 433–438.
    • (2008) ChemBioChem , vol.9 , pp. 433-438
    • Tarling, C.A.1    Woods, K.2    Zhang, R.3
  • 65
    • 84930485840 scopus 로고    scopus 로고
    • Hypolipidemic and bifidogenic potentials in the dietary fiber prepared from mikan (Japanese mandarin orange: Citrus unshiu) albedo
    • Iwata, E., H. Hotta & M. Goto. 2012. Hypolipidemic and bifidogenic potentials in the dietary fiber prepared from mikan (Japanese mandarin orange: Citrus unshiu) albedo. J. Nutr. Sci. Vitaminol. 58: 175–180.
    • (2012) J. Nutr. Sci. Vitaminol. , vol.58 , pp. 175-180
    • Iwata, E.1    Hotta, H.2    Goto, M.3
  • 66
    • 58449124786 scopus 로고    scopus 로고
    • Inhibitory effect of pectin from the segment membrane of citrus fruits on lipase activity
    • Edashige, Y., N. Murakami & T. Tsujita. 2008. Inhibitory effect of pectin from the segment membrane of citrus fruits on lipase activity. J. Nutr. Sci. Vitaminol. 54: 409–415.
    • (2008) J. Nutr. Sci. Vitaminol. , vol.54 , pp. 409-415
    • Edashige, Y.1    Murakami, N.2    Tsujita, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.