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Volumn 53, Issue 7, 2014, Pages 1465-1474

Lactobacillus strains isolated from infant faeces possess potent inhibitory activity against intestinal alpha- and beta-glucosidases suggesting anti-diabetic potential

Author keywords

Alpha glucosidase; Beta glucosidase; Lactobacillus

Indexed keywords

ACARBOSE; ALPHA GLUCOSIDASE; ALPHA GLUCOSIDASE INHIBITOR; AMYLASE; ANTIDIABETIC AGENT; BACTERIAL EXTRACT; BETA GLUCOSIDASE INHIBITOR; GLUCOSE; GLYCOSIDASE INHIBITOR; LACTASE; SUCRASE; SUCROSE; UNCLASSIFIED DRUG; BACTERIAL DNA; BETA GLUCOSIDASE; ENZYME INHIBITOR; GLUCOSE BLOOD LEVEL; PROBIOTIC AGENT;

EID: 84918799724     PISSN: 14366207     EISSN: 14366215     Source Type: Journal    
DOI: 10.1007/s00394-013-0649-9     Document Type: Article
Times cited : (115)

References (37)
  • 1
    • 84857082127 scopus 로고    scopus 로고
    • α-Amylase inhibitors: a review of raw material and isolated compounds from plant source
    • Sales PM, Souza PM, Simeoni LA, Magalhaes PO, Silveira D (2012) α-Amylase inhibitors: a review of raw material and isolated compounds from plant source. J Pharm Pharm Sci 15(1):141–183
    • (2012) J Pharm Pharm Sci , vol.15 , Issue.1 , pp. 141-183
    • Sales, P.M.1    Souza, P.M.2    Simeoni, L.A.3    Magalhaes, P.O.4    Silveira, D.5
  • 2
    • 84876768363 scopus 로고    scopus 로고
    • Inhibitory effect of Azadirachta indica A. Juss leaf extract on the activities of α-amylase and α-glucosidase
    • COI: 1:STN:280:DC%2BC2cvktVGqtQ%3D%3D
    • Kazeem MI, Dansu TV, Adeola SA (2013) Inhibitory effect of Azadirachta indica A. Juss leaf extract on the activities of α-amylase and α-glucosidase. Pak J Biol Sci 16(21):1358–1362
    • (2013) Pak J Biol Sci , vol.16 , Issue.21 , pp. 1358-1362
    • Kazeem, M.I.1    Dansu, T.V.2    Adeola, S.A.3
  • 3
    • 0030755109 scopus 로고    scopus 로고
    • Alpha-glucosidase inhibitors
    • COI: 1:CAS:528:DyaK2sXms12gt74%3D
    • Lebovitz HE (1997) Alpha-glucosidase inhibitors. Endocrinol Metab Clin 26(3):539–551
    • (1997) Endocrinol Metab Clin , vol.26 , Issue.3 , pp. 539-551
    • Lebovitz, H.E.1
  • 4
    • 84869752516 scopus 로고    scopus 로고
    • α-Glucosidase inhibitors and their use in clinical practice
    • COI: 1:CAS:528:DC%2BC3sXitVCluro%3D
    • Derosa G, Maffioli P (2012) α-Glucosidase inhibitors and their use in clinical practice. Arch Med Sci 8(5):899–906
    • (2012) Arch Med Sci , vol.8 , Issue.5 , pp. 899-906
    • Derosa, G.1    Maffioli, P.2
  • 5
    • 0032855459 scopus 로고    scopus 로고
    • Effects of the α-glucosidase inhibitor acarbose on the development of long term complications in diabetic animals: pathophysiological and therapeutic implications
    • COI: 1:CAS:528:DyaK1MXmsl2gtrc%3D
    • Creutzfeldt W (1999) Effects of the α-glucosidase inhibitor acarbose on the development of long term complications in diabetic animals: pathophysiological and therapeutic implications. Diabetes Metab Res Rev 15:289–296
    • (1999) Diabetes Metab Res Rev , vol.15 , pp. 289-296
    • Creutzfeldt, W.1
  • 6
    • 84863482399 scopus 로고    scopus 로고
    • Alpha-glucosidase inhibitors 2012—cardio vascular considerations and trial evaluation
    • Standl E, Schnell O (2012) Alpha-glucosidase inhibitors 2012—cardio vascular considerations and trial evaluation. Diabetes Vasc Dis Res 9(3):163–169
    • (2012) Diabetes Vasc Dis Res , vol.9 , Issue.3 , pp. 163-169
    • Standl, E.1    Schnell, O.2
  • 7
    • 84884555025 scopus 로고    scopus 로고
    • Antiviral therapies targeting host ER alpha-glucosidases: current status and future directions
    • COI: 1:CAS:528:DC%2BC3sXhsFenurrL
    • Chang J, Block TM, Guo JT (2013) Antiviral therapies targeting host ER alpha-glucosidases: current status and future directions. Antivir Res 99(3):251–260
    • (2013) Antivir Res , vol.99 , Issue.3 , pp. 251-260
    • Chang, J.1    Block, T.M.2    Guo, J.T.3
  • 8
    • 84872311972 scopus 로고    scopus 로고
    • Critical evaluation of the role of acarbose in the treatment of diabetes: patient considerations
    • COI: 1:CAS:528:DC%2BC38Xhs1WhurbM
    • Rosak C, Mertes G (2012) Critical evaluation of the role of acarbose in the treatment of diabetes: patient considerations. Diabetes Metab Syndr Obes 5:357–367
    • (2012) Diabetes Metab Syndr Obes , vol.5 , pp. 357-367
    • Rosak, C.1    Mertes, G.2
  • 9
    • 84862122513 scopus 로고    scopus 로고
    • Efficacy and safety profile evaluation of acarbose alone and in association with other antidiabetic drugs: a systematic review
    • COI: 1:CAS:528:DC%2BC38XosVGqtb0%3D
    • Derosa G, Maffioli P (2012) Efficacy and safety profile evaluation of acarbose alone and in association with other antidiabetic drugs: a systematic review. Clin Ther 34(6):1221–1236
    • (2012) Clin Ther , vol.34 , Issue.6 , pp. 1221-1236
    • Derosa, G.1    Maffioli, P.2
  • 11
    • 0037097039 scopus 로고    scopus 로고
    • Acarbose for prevention of type 2 diabetes mellitus: the STOP-NIDDM randomised trial
    • COI: 1:CAS:528:DC%2BD38XkslGhs7g%3D
    • Chiasson JL, Josse RG, Gomis R, Hanefeld M, Karasik A, Laakso M (2002) Acarbose for prevention of type 2 diabetes mellitus: the STOP-NIDDM randomised trial. Lancet 359:2072–2077
    • (2002) Lancet , vol.359 , pp. 2072-2077
    • Chiasson, J.L.1    Josse, R.G.2    Gomis, R.3    Hanefeld, M.4    Karasik, A.5    Laakso, M.6
  • 12
    • 84856203305 scopus 로고    scopus 로고
    • Inhibitory effect of dates-extract on α-amylase and β-glucosidase enzymes relevant to non-insulin dependent diabetes mellitus
    • COI: 1:CAS:528:DC%2BC3cXht12lt77N
    • Al-Zuhair S, Dowaidar A, Kamal H (2010) Inhibitory effect of dates-extract on α-amylase and β-glucosidase enzymes relevant to non-insulin dependent diabetes mellitus. J Biochem Tech 2(2):158–160
    • (2010) J Biochem Tech , vol.2 , Issue.2 , pp. 158-160
    • Al-Zuhair, S.1    Dowaidar, A.2    Kamal, H.3
  • 13
    • 77956629122 scopus 로고    scopus 로고
    • Natural products as alpha-amylase and alpha-glucosidase inhibitors and their hypoglycaemic potential in the treatment of diabetes: an update
    • COI: 1:CAS:528:DC%2BC3cXnt1Kru78%3D
    • Tundis R, Loizzo MR, Menichini F (2010) Natural products as alpha-amylase and alpha-glucosidase inhibitors and their hypoglycaemic potential in the treatment of diabetes: an update. Mini Rev Med Chem 10(4):315–331
    • (2010) Mini Rev Med Chem , vol.10 , Issue.4 , pp. 315-331
    • Tundis, R.1    Loizzo, M.R.2    Menichini, F.3
  • 14
    • 84867053639 scopus 로고    scopus 로고
    • Potent α-glucosidase and α-amylase inhibitory activities of standardized 50% ethanolic extracts and sinensetin from Orthosiphonstamineus Benth as anti-diabetic mechanism
    • COI: 1:CAS:528:DC%2BC3sXhsFOqt7c%3D
    • Mohamed ELH, Siddiqui MJA, Ang LF, Sadikun A, Chan SH, Tan SC, Asmawi MZ, Yam MF (2012) Potent α-glucosidase and α-amylase inhibitory activities of standardized 50% ethanolic extracts and sinensetin from Orthosiphonstamineus Benth as anti-diabetic mechanism. BMC Complement Altern Med 12:176
    • (2012) BMC Complement Altern Med , vol.12 , pp. 176
    • Mohamed, E.L.H.1    Siddiqui, M.J.A.2    Ang, L.F.3    Sadikun, A.4    Chan, S.H.5    Tan, S.C.6    Asmawi, M.Z.7    Yam, M.F.8
  • 15
    • 84887918281 scopus 로고    scopus 로고
    • In vitro studies on alpha amylase and alpha glucosidase inhibitory activities of selected plant extracts
    • Nair SS, Kavrekar V, Mishra A (2013) In vitro studies on alpha amylase and alpha glucosidase inhibitory activities of selected plant extracts. Eur J Exp Biol 3(1):128–132
    • (2013) Eur J Exp Biol , vol.3 , Issue.1 , pp. 128-132
    • Nair, S.S.1    Kavrekar, V.2    Mishra, A.3
  • 16
    • 84886422192 scopus 로고    scopus 로고
    • α-Glucosidase and α-amylase inhibitory activities of Pithecellobium dulce bark and leaves
    • Katekhaye SD, Nagmoti DM (2013) α-Glucosidase and α-amylase inhibitory activities of Pithecellobium dulce bark and leaves. Phytopharmacology 4(1):123–130
    • (2013) Phytopharmacology , vol.4 , Issue.1 , pp. 123-130
    • Katekhaye, S.D.1    Nagmoti, D.M.2
  • 17
    • 34250678991 scopus 로고    scopus 로고
    • Chemistry, physiological properties, and microbial production of hydroxycitric acid
    • COI: 1:CAS:528:DC%2BD2sXmsVKqsbs%3D
    • Yamada T, Hida H, Yamada Y (2007) Chemistry, physiological properties, and microbial production of hydroxycitric acid. Appl Microbiol Biotechnol 75(5):977–982
    • (2007) Appl Microbiol Biotechnol , vol.75 , Issue.5 , pp. 977-982
    • Yamada, T.1    Hida, H.2    Yamada, Y.3
  • 19
    • 39749127715 scopus 로고    scopus 로고
    • Proteolytic profiles and angiotensin-1 converting enzyme and alpha-glucosidase inhibitory activities of selected lactic acid bacteria
    • COI: 1:CAS:528:DC%2BD1cXitlyks7w%3D
    • Ramchandran L, Shah NP (2008) Proteolytic profiles and angiotensin-1 converting enzyme and alpha-glucosidase inhibitory activities of selected lactic acid bacteria. J Food Sci 73(2):M75–M81
    • (2008) J Food Sci , vol.73 , Issue.2 , pp. M75-M81
    • Ramchandran, L.1    Shah, N.P.2
  • 20
    • 84873432002 scopus 로고    scopus 로고
    • Probiotics as potential biotherapeutics in the management of type 2 diabetes—prospects and perspectives
    • COI: 1:CAS:528:DC%2BC3sXit1WhtL0%3D
    • Panwar H, Rashmi HM, Batish VK, Grover S (2013) Probiotics as potential biotherapeutics in the management of type 2 diabetes—prospects and perspectives. Diabetes Metab Res Rev 29:103–112
    • (2013) Diabetes Metab Res Rev , vol.29 , pp. 103-112
    • Panwar, H.1    Rashmi, H.M.2    Batish, V.K.3    Grover, S.4
  • 21
    • 84860003661 scopus 로고    scopus 로고
    • A meta-analysis of probiotic efficacy for gastrointestinal diseases
    • COI: 1:CAS:528:DC%2BC38XmsVGgtbk%3D
    • Ritchie ML, Romanuk TN (2012) A meta-analysis of probiotic efficacy for gastrointestinal diseases. PLoS One 7(4):e34938
    • (2012) PLoS One , vol.7 , Issue.4 , pp. e34938
    • Ritchie, M.L.1    Romanuk, T.N.2
  • 22
    • 33846928981 scopus 로고    scopus 로고
    • Spotlight on VSL#3 probiotic mixture in chronic inflammatory bowel diseases
    • COI: 1:CAS:528:DC%2BD2sXjt1SgtLo%3D
    • Chapman TM, Plosker GL, Figgitt DP (2007) Spotlight on VSL#3 probiotic mixture in chronic inflammatory bowel diseases. Bio Drugs 21(1):61–63
    • (2007) Bio Drugs , vol.21 , Issue.1 , pp. 61-63
    • Chapman, T.M.1    Plosker, G.L.2    Figgitt, D.P.3
  • 23
    • 84918842077 scopus 로고    scopus 로고
    • Anonymous or Sigma Tau Pharmaceuticals Inc. (2011) VSL#3 double strength product information sheet
    • Anonymous or Sigma Tau Pharmaceuticals Inc. (2011) VSL#3 double strength product information sheet. http://www.vsl3.com/pdf/VSL3_DS_PL.pdf
  • 24
    • 0037057121 scopus 로고    scopus 로고
    • A PCR based method for identification of lactobacilli at the genus level
    • COI: 1:CAS:528:DC%2BD38Xnt1Kmu74%3D
    • Dubernet S, Desmasures N, Gueguen M (2002) A PCR based method for identification of lactobacilli at the genus level. FEMS Microbiol Lett 214(2):271–275
    • (2002) FEMS Microbiol Lett , vol.214 , Issue.2 , pp. 271-275
    • Dubernet, S.1    Desmasures, N.2    Gueguen, M.3
  • 25
    • 0033166540 scopus 로고    scopus 로고
    • Investigating deep phylogenetic relationships among cyanobacteria and plastids by small subunit rRNA sequence analysis
    • COI: 1:CAS:528:DyaK1MXlslSlu7Y%3D
    • Turner S, Pryer KM, Miao VPW, Palmer JD (1999) Investigating deep phylogenetic relationships among cyanobacteria and plastids by small subunit rRNA sequence analysis. J Eukaryot Microbiol 46:327–338
    • (1999) J Eukaryot Microbiol , vol.46 , pp. 327-338
    • Turner, S.1    Pryer, K.M.2    Miao, V.P.W.3    Palmer, J.D.4
  • 26
    • 0025013355 scopus 로고
    • Towards a phylogeny and definition of species at the molecular level within the genus Mycobacterium
    • COI: 1:CAS:528:DyaK3MXhtFyitLg%3D
    • Rogall TJ, Wolters TF, Bottger EC (1990) Towards a phylogeny and definition of species at the molecular level within the genus Mycobacterium. Int J Syst Bacteriol 40:323–330
    • (1990) Int J Syst Bacteriol , vol.40 , pp. 323-330
    • Rogall, T.J.1    Wolters, T.F.2    Bottger, E.C.3
  • 29
    • 84880844177 scopus 로고    scopus 로고
    • Inhibitory effect of components from Streptomyces species on alpha-glucosidase and alpha-amylase of different origin
    • COI: 1:STN:280:DC%2BC3sjltlaisA%3D%3D
    • Meng P, Xie C, Geng P, Qi X, Zheng F, Bai F (2013) Inhibitory effect of components from Streptomyces species on alpha-glucosidase and alpha-amylase of different origin. Prikl Biokhim Mikrobiol 49(2):181–189
    • (2013) Prikl Biokhim Mikrobiol , vol.49 , Issue.2 , pp. 181-189
    • Meng, P.1    Xie, C.2    Geng, P.3    Qi, X.4    Zheng, F.5    Bai, F.6
  • 30
    • 84870690308 scopus 로고    scopus 로고
    • Production of the α-glycosidase inhibitor 1-deoxynojirimycin from Bacillus species
    • COI: 1:CAS:528:DC%2BC38XhvVyru7fN
    • Onose S, Ikeda R, Nakagawa K, Kimura T, Yamagishi K, Higuchi O, Miyazawa T (2013) Production of the α-glycosidase inhibitor 1-deoxynojirimycin from Bacillus species. Food Chem 138(1):516–523
    • (2013) Food Chem , vol.138 , Issue.1 , pp. 516-523
    • Onose, S.1    Ikeda, R.2    Nakagawa, K.3    Kimura, T.4    Yamagishi, K.5    Higuchi, O.6    Miyazawa, T.7
  • 31
    • 84867653534 scopus 로고    scopus 로고
    • Expression and purification of two Family GH31 α-glucosidases from Bacteroides thetaiotaomicron
    • COI: 1:CAS:528:DC%2BC38Xhs1GqtLnI
    • Chaudet MM, Allen JL, Rose DR (2012) Expression and purification of two Family GH31 α-glucosidases from Bacteroides thetaiotaomicron. Protein Expr Purif 86(2):135–141
    • (2012) Protein Expr Purif , vol.86 , Issue.2 , pp. 135-141
    • Chaudet, M.M.1    Allen, J.L.2    Rose, D.R.3
  • 32
    • 32944466887 scopus 로고    scopus 로고
    • Ecological and evolutionary forces shaping microbial diversity in the human intestine
    • COI: 1:CAS:528:DC%2BD28Xit1Kltbs%3D
    • Ley RE, Peterson DA, Gordon JI (2006) Ecological and evolutionary forces shaping microbial diversity in the human intestine. Cell 124:837–848
    • (2006) Cell , vol.124 , pp. 837-848
    • Ley, R.E.1    Peterson, D.A.2    Gordon, J.I.3
  • 33
    • 80051856839 scopus 로고    scopus 로고
    • The human gut microbiome: ecology and recent evolutionary changes
    • COI: 1:CAS:528:DC%2BC3MXhsVSrtLbO
    • Walter J, Ley R (2011) The human gut microbiome: ecology and recent evolutionary changes. Annu Rev Microbiol 65:411–429
    • (2011) Annu Rev Microbiol , vol.65 , pp. 411-429
    • Walter, J.1    Ley, R.2
  • 34
    • 67349281229 scopus 로고    scopus 로고
    • Effects of Lactobacillus acidophilus on gut microflora metabolic biomarkers in fed and fasted rats
    • COI: 1:CAS:528:DC%2BD1MXntVKgtb8%3D
    • Mountzouris KC, Kotzampassi K, Tsirtsikos P, Kapoutzis K, Fegeros K (2009) Effects of Lactobacillus acidophilus on gut microflora metabolic biomarkers in fed and fasted rats. Clin Nutr 28(3):318–324
    • (2009) Clin Nutr , vol.28 , Issue.3 , pp. 318-324
    • Mountzouris, K.C.1    Kotzampassi, K.2    Tsirtsikos, P.3    Kapoutzis, K.4    Fegeros, K.5
  • 35
    • 84859269737 scopus 로고    scopus 로고
    • Screening for glycosidase activities of lactic acid bacteria as a biotechnological tool in oenology
    • Perez-Martín F, Sesena S, Izquierdo PM, Martín R, Palop ML (2012) Screening for glycosidase activities of lactic acid bacteria as a biotechnological tool in oenology. World J Microbiol Biotechnol 28(4):1423–1432
    • (2012) World J Microbiol Biotechnol , vol.28 , Issue.4 , pp. 1423-1432
    • Perez-Martín, F.1    Sesena, S.2    Izquierdo, P.M.3    Martín, R.4    Palop, M.L.5
  • 36
    • 37549048013 scopus 로고    scopus 로고
    • Influence of alternansucrase-derived oligosaccharides and other carbohydrates on alpha-galactosidase and alpha-glucosidase activity in Bifidobacterium adolescentis
    • COI: 1:CAS:528:DC%2BD1cXisFSit7o%3D
    • Holt SM, Teresi JM, Cote GL (2008) Influence of alternansucrase-derived oligosaccharides and other carbohydrates on alpha-galactosidase and alpha-glucosidase activity in Bifidobacterium adolescentis. Lett Appl Microbiol 46(1):73–79
    • (2008) Lett Appl Microbiol , vol.46 , Issue.1 , pp. 73-79
    • Holt, S.M.1    Teresi, J.M.2    Cote, G.L.3
  • 37
    • 84873686302 scopus 로고    scopus 로고
    • Enzymatic properties of a thermostable α-glucosidase from acidothermophilic crenarchaeon Sulfolobus tokodaii strain 7
    • COI: 1:CAS:528:DC%2BC3sXjtlGnt7s%3D
    • Park JE, Park SH, Woo JY, Hwang HS, Cha J, Lee H (2013) Enzymatic properties of a thermostable α-glucosidase from acidothermophilic crenarchaeon Sulfolobus tokodaii strain 7. J Microbiol Biotechnol 23(1):56–63
    • (2013) J Microbiol Biotechnol , vol.23 , Issue.1 , pp. 56-63
    • Park, J.E.1    Park, S.H.2    Woo, J.Y.3    Hwang, H.S.4    Cha, J.5    Lee, H.6


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