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Volumn 54, Issue 8, 2014, Pages 802-811

Halotolerant, acid-alkali stable, chelator resistant and raw starch digesting α-amylase from a marine bacterium Bacillus subtilis S8-18

Author keywords

Alpha amylase; Bacillus subtilis; Characterization; Halotolerant; Raw starch

Indexed keywords

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS);

EID: 84906259217     PISSN: 0233111X     EISSN: 15214028     Source Type: Journal    
DOI: 10.1002/jobm.201200732     Document Type: Article
Times cited : (27)

References (55)
  • 4
    • 77955242147 scopus 로고    scopus 로고
    • Hyper-production of alpha-amylase from agro-residual medium with high-glucose in SSF using catabolite derepressed Bacillus subtilis KCC103
    • Rajagopalan, G., Krishnan, C., 2010. Hyper-production of alpha-amylase from agro-residual medium with high-glucose in SSF using catabolite derepressed Bacillus subtilis KCC103. J. Basic Microbiol., 50, 336-343.
    • (2010) J. Basic Microbiol. , vol.50 , pp. 336-343
    • Rajagopalan, G.1    Krishnan, C.2
  • 5
    • 0035924187 scopus 로고    scopus 로고
    • Production of starch gel digesting amyloglucosidase by Aspergillus oryzae HS-3 in solid state fermentation
    • Singh, H., Soni, S.K., 2001. Production of starch gel digesting amyloglucosidase by Aspergillus oryzae HS-3 in solid state fermentation. Process Biochem., 37, 453-459.
    • (2001) Process Biochem. , vol.37 , pp. 453-459
    • Singh, H.1    Soni, S.K.2
  • 6
    • 25444445001 scopus 로고    scopus 로고
    • A novel raw starch digesting thermostable α-amylase from Bacillus sp. I-3 and its use in the direct hydrolysis of raw potato starch
    • Goyal, N., Gupta, J.K., Soni, S.K., 2005. A novel raw starch digesting thermostable α-amylase from Bacillus sp. I-3 and its use in the direct hydrolysis of raw potato starch. Enzyme Microb. Technol., 37, 723-734.
    • (2005) Enzyme Microb. Technol. , vol.37 , pp. 723-734
    • Goyal, N.1    Gupta, J.K.2    Soni, S.K.3
  • 7
    • 15744390105 scopus 로고    scopus 로고
    • α-Amylase from B. amyloliquefaciens: purification, characterization, raw starch degradation and expression in E. coli
    • Demirkan, E.S., Mikami, B., Adachi, M., Higasa, T., Utsumi, S., 2005. α-Amylase from B. amyloliquefaciens: purification, characterization, raw starch degradation and expression in E. coli. Process Biochem., 40, 2629-2636.
    • (2005) Process Biochem. , vol.40 , pp. 2629-2636
    • Demirkan, E.S.1    Mikami, B.2    Adachi, M.3    Higasa, T.4    Utsumi, S.5
  • 8
    • 40749092049 scopus 로고    scopus 로고
    • A novel raw starch digesting α-amylase from a newly isolated Bacillus sp. YX-1: purification and characterization
    • Liu, X.D., Xu, Y., 2008. A novel raw starch digesting α-amylase from a newly isolated Bacillus sp. YX-1: purification and characterization. Bioresour. Technol., 99, 4315-4320.
    • (2008) Bioresour. Technol. , vol.99 , pp. 4315-4320
    • Liu, X.D.1    Xu, Y.2
  • 9
    • 0033958836 scopus 로고    scopus 로고
    • Comparison of degradation abilities of α and β-amylases on raw starch granules
    • Sarikaya, E., Higasa, T., Adachi, M., Mikamib, B., 2000. Comparison of degradation abilities of α and β-amylases on raw starch granules. Process Biochem., 35, 711-715.
    • (2000) Process Biochem. , vol.35 , pp. 711-715
    • Sarikaya, E.1    Higasa, T.2    Adachi, M.3    Mikamib, B.4
  • 10
    • 70350545548 scopus 로고    scopus 로고
    • Biochemical characterization of a raw starch degrading α-amylase from the Indonesian marine bacterium Bacillus sp. ALSHL3
    • Vidilaseris, K., Hidayat, K., Retnoningrum, D.S., Nurachman, Z., et al., 2009. Biochemical characterization of a raw starch degrading α-amylase from the Indonesian marine bacterium Bacillus sp. ALSHL3. Biologia, 64, 1047-1052.
    • (2009) Biologia , vol.64 , pp. 1047-1052
    • Vidilaseris, K.1    Hidayat, K.2    Retnoningrum, D.S.3    Nurachman, Z.4
  • 11
    • 79960089100 scopus 로고    scopus 로고
    • Identification a novel raw-starch-degrading-α-amylase from a tropical marine bacterium
    • Nurachman, Z., Kono, A., Radjasa, O.K., Natalia, D., 2010. Identification a novel raw-starch-degrading-α-amylase from a tropical marine bacterium. Am. J. Biochem. Biotechnol., 6, 300-306.
    • (2010) Am. J. Biochem. Biotechnol. , vol.6 , pp. 300-306
    • Nurachman, Z.1    Kono, A.2    Radjasa, O.K.3    Natalia, D.4
  • 12
  • 13
    • 84861659828 scopus 로고    scopus 로고
    • Purification and characterization of maltooligosaccharide-forming α-amylase from moderately halophilic Marinobacter sp EMB8
    • Kumar, S., Khare, S.K., 2012. Purification and characterization of maltooligosaccharide-forming α-amylase from moderately halophilic Marinobacter sp EMB8. Bioresour. Technol., 116, 247-251.
    • (2012) Bioresour. Technol. , vol.116 , pp. 247-251
    • Kumar, S.1    Khare, S.K.2
  • 14
    • 0028958071 scopus 로고
    • Structural features that stabilize halophilicmalate dehydogenase from archaebacterium
    • Dym, O., Mavarech, M., Sussam, J.L., 1995. Structural features that stabilize halophilicmalate dehydogenase from archaebacterium. Science, 267, 1344-1346.
    • (1995) Science , vol.267 , pp. 1344-1346
    • Dym, O.1    Mavarech, M.2    Sussam, J.L.3
  • 15
    • 54349101266 scopus 로고    scopus 로고
    • Highly thermostable and alkaline α-amylase from a halotolerant alkaliphilic Bacillus sp. AB68
    • Aygan, A., Arikan, B., Korkmaz, H., Dincer, S., Colak, O., 2008. Highly thermostable and alkaline α-amylase from a halotolerant alkaliphilic Bacillus sp. AB68. Braz. J. Microbiol., 39, 547-553.
    • (2008) Braz. J. Microbiol. , vol.39 , pp. 547-553
    • Aygan, A.1    Arikan, B.2    Korkmaz, H.3    Dincer, S.4    Colak, O.5
  • 16
    • 0030668247 scopus 로고    scopus 로고
    • Thermostable, salt-tolerant α-amylase from Bacillus sp. MD 124
    • Jana, M., Pati, B., 1997. Thermostable, salt-tolerant α-amylase from Bacillus sp. MD 124. J. Basic Microbiol., 37, 323-326.
    • (1997) J. Basic Microbiol. , vol.37 , pp. 323-326
    • Jana, M.1    Pati, B.2
  • 17
    • 77956415992 scopus 로고    scopus 로고
    • Isolation of heterotrophic bacteria from Palk Bay sediments showing heavy metal tolerance and antibiotic production
    • Nithya, C., Pandian, S.K., 2009. Isolation of heterotrophic bacteria from Palk Bay sediments showing heavy metal tolerance and antibiotic production. Microbiol. Res., 165, 578-593.
    • (2009) Microbiol. Res. , vol.165 , pp. 578-593
    • Nithya, C.1    Pandian, S.K.2
  • 18
    • 84866360434 scopus 로고    scopus 로고
    • Antibiofilm activity of α-amylase from Bacillus subtilis S8-18 against biofilm forming human bacterial pathogens
    • Kalpana, B.J., Aarthy, S., Pandian, S.K., 2012. Antibiofilm activity of α-amylase from Bacillus subtilis S8-18 against biofilm forming human bacterial pathogens. Appl. Biochem. Biotechnol., 167, 1778-1794.
    • (2012) Appl. Biochem. Biotechnol. , vol.167 , pp. 1778-1794
    • Kalpana, B.J.1    Aarthy, S.2    Pandian, S.K.3
  • 19
    • 33846158433 scopus 로고    scopus 로고
    • Partial characterization and optimization of extra-cellular α-amylase from Bacillus subtilis isolated from cow dung microflora
    • Swain, M.R., Kar, S., Padmaja, G., Ray, R.C., 2006. Partial characterization and optimization of extra-cellular α-amylase from Bacillus subtilis isolated from cow dung microflora. Polish J. Microbiol., 55, 289-296.
    • (2006) Polish J. Microbiol. , vol.55 , pp. 289-296
    • Swain, M.R.1    Kar, S.2    Padmaja, G.3    Ray, R.C.4
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 52449123053 scopus 로고    scopus 로고
    • 2+-independent, raw-starch hydrolysing α-amylase from Bacillus sp. GRE1: characterization and gene isolation
    • 2+-independent, raw-starch hydrolysing α-amylase from Bacillus sp. GRE1: characterization and gene isolation. World J. Microbiol. Biotechnol., 24, 2517-2524.
    • (2008) World J. Microbiol. Biotechnol. , vol.24 , pp. 2517-2524
    • Haki, G.D.1    Anceno, A.J.2    Rakshit, S.K.3
  • 23
  • 24
    • 41549139096 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a novel a-amylase from Bacillus licheniformis NH1 Cloning, nucleotide sequence and expression of amyN gene in Escherichia coli
    • Hmidet, N., Bayoudh, A., Berrin, J.G., Kanoun, S., et al., 2008. Purification and biochemical characterization of a novel a-amylase from Bacillus licheniformis NH1 Cloning, nucleotide sequence and expression of amyN gene in Escherichia coli. Process Biochem., 43, 499-510.
    • (2008) Process Biochem. , vol.43 , pp. 499-510
    • Hmidet, N.1    Bayoudh, A.2    Berrin, J.G.3    Kanoun, S.4
  • 26
    • 33748037939 scopus 로고
    • Amylases α- and β-methods
    • Bernfeld, P., 1955. Amylases α- and β-methods. Enzymology, 1, 149-158.
    • (1955) Enzymology , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 27
    • 77950368090 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a novel SDS and surfactant stable, raw starch digesting, and halophilic α-amylase from a moderately halophilic bacterium, Nesterenkonia sp. strain F
    • Shafiei, M., Ziaee, A., Amoozegar, M., 2010. Purification and biochemical characterization of a novel SDS and surfactant stable, raw starch digesting, and halophilic α-amylase from a moderately halophilic bacterium, Nesterenkonia sp. strain F. Process Biochem., 45, 694-699.
    • (2010) Process Biochem. , vol.45 , pp. 694-699
    • Shafiei, M.1    Ziaee, A.2    Amoozegar, M.3
  • 28
    • 0030321729 scopus 로고    scopus 로고
    • Thermostable alpha-amylase production using Bacillus licheniformis NRRL B14368
    • Bose, K., Das, D., 1996. Thermostable alpha-amylase production using Bacillus licheniformis NRRL B14368. Indian J. Exp. Biol., 34, 1279-1282.
    • (1996) Indian J. Exp. Biol. , vol.34 , pp. 1279-1282
    • Bose, K.1    Das, D.2
  • 30
    • 1642283662 scopus 로고    scopus 로고
    • A thermostable maltose-tolerant α-amylase from Aspergillus tamarii
    • Moreira, F.G., Lenartovicz, V., Peralta, R.M., 2004. A thermostable maltose-tolerant α-amylase from Aspergillus tamarii. J. Basic Microbiol., 44, 29-35.
    • (2004) J. Basic Microbiol. , vol.44 , pp. 29-35
    • Moreira, F.G.1    Lenartovicz, V.2    Peralta, R.M.3
  • 31
    • 14544282884 scopus 로고    scopus 로고
    • A Ca-independent alpha-amylase that is active and stable at low pH from the Bacillus sp. KR-8104
    • Sajedi, R.H., Naderi-Manesh, H., Khajeh, K., Ahmadvand, R., et al., 2005. A Ca-independent alpha-amylase that is active and stable at low pH from the Bacillus sp. KR-8104. Enzyme Microb. Technol., 36, 666-671.
    • (2005) Enzyme Microb. Technol. , vol.36 , pp. 666-671
    • Sajedi, R.H.1    Naderi-Manesh, H.2    Khajeh, K.3    Ahmadvand, R.4
  • 32
    • 79951485865 scopus 로고    scopus 로고
    • Purification and characterization of a novel alkali-stable α-amylase from Chryseobacterium taeanense TKU001 and application in antioxidant and prebiotic
    • Wang, S.L., Liang, Y.C., Liang, T.W., 2011. Purification and characterization of a novel alkali-stable α-amylase from Chryseobacterium taeanense TKU001 and application in antioxidant and prebiotic. Process Biochem., 46, 745-750.
    • (2011) Process Biochem. , vol.46 , pp. 745-750
    • Wang, S.L.1    Liang, Y.C.2    Liang, T.W.3
  • 33
    • 68649106159 scopus 로고    scopus 로고
    • Characterization of thermo-tolerant and acid/alkali tolerant β-glucosidase from bacterial isolate M+
    • Bajaj, B.K., Pangotra, H., Wani, M.A., Sharma, A., Sharma, P., 2009. Characterization of thermo-tolerant and acid/alkali tolerant β-glucosidase from bacterial isolate M+. J. Sci. Ind. Res., 68, 242-247.
    • (2009) J. Sci. Ind. Res. , vol.68 , pp. 242-247
    • Bajaj, B.K.1    Pangotra, H.2    Wani, M.A.3    Sharma, A.4    Sharma, P.5
  • 34
    • 0035318737 scopus 로고    scopus 로고
    • Novel amylase that is highly resistant to chelating reagents and chemical oxidants from the Alkaliphilic Bacillus sp. isolate KSM-K38
    • Hagihara, H., Igarashi, K., Hayashi, Y., Endo, K., et al., 2001. Novel amylase that is highly resistant to chelating reagents and chemical oxidants from the Alkaliphilic Bacillus sp. isolate KSM-K38. Appl. Environ. Microbiol., 67, 1744-1750.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1744-1750
    • Hagihara, H.1    Igarashi, K.2    Hayashi, Y.3    Endo, K.4
  • 36
    • 0038613858 scopus 로고    scopus 로고
    • Enzymatic properties of novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6
    • Burhan, A., Nisa, U., Gokhan, C., Omer, C., et al., 2003. Enzymatic properties of novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6. Process Biochem., 38, 1397-1403.
    • (2003) Process Biochem. , vol.38 , pp. 1397-1403
    • Burhan, A.1    Nisa, U.2    Gokhan, C.3    Omer, C.4
  • 37
    • 37449020231 scopus 로고    scopus 로고
    • Production of surfactant and detergent stable, halophilic and alkali tolerant α-amylase by a moderately halophilic Bacillus sp. strain TSCVKK
    • Kiran, K.K., Chandra, T.S., 2008. Production of surfactant and detergent stable, halophilic and alkali tolerant α-amylase by a moderately halophilic Bacillus sp. strain TSCVKK, Appl. Microbiol. Biotechnol., 77, 1023-1031.
    • (2008) Appl. Microbiol. Biotechnol. , vol.77 , pp. 1023-1031
    • Kiran, K.K.1    Chandra, T.S.2
  • 38
    • 0021892611 scopus 로고
    • The mechanisms of irreversible enzyme inactivation at 100°C
    • Ahern, T.J., Klibanov, A.M., 1985. The mechanisms of irreversible enzyme inactivation at 100°C. Science, 228, 1280-1284.
    • (1985) Science , vol.228 , pp. 1280-1284
    • Ahern, T.J.1    Klibanov, A.M.2
  • 39
    • 0035066633 scopus 로고    scopus 로고
    • Enzymic properties of a SDS-resistant Bacillus sp. TS-23 α-amylase produced by recombinant Escherichia coli
    • Lo, H.F., Lin, L.L., Chen, H.L., Hsu, W.H., Chang, C.T., 2001. Enzymic properties of a SDS-resistant Bacillus sp. TS-23 α-amylase produced by recombinant Escherichia coli. Process Biochem., 36, 743-750.
    • (2001) Process Biochem. , vol.36 , pp. 743-750
    • Lo, H.F.1    Lin, L.L.2    Chen, H.L.3    Hsu, W.H.4    Chang, C.T.5
  • 40
    • 3142642544 scopus 로고    scopus 로고
    • Purification and properties of a maltotriose-producing α-amylase from Thermobifida fusca
    • Yang, C.H., Liu, W.H., 2004. Purification and properties of a maltotriose-producing α-amylase from Thermobifida fusca. Enzyme Microb. Technol., 35, 254-260.
    • (2004) Enzyme Microb. Technol. , vol.35 , pp. 254-260
    • Yang, C.H.1    Liu, W.H.2
  • 41
    • 64249084104 scopus 로고    scopus 로고
    • Immobilized bacterial α-amylase for effective hydrolysis of raw and soluble starch
    • Gangadharan, D., Nampoothiri, K.M., Sivaramakrishnan, S., Pandey, A., 2009. Immobilized bacterial α-amylase for effective hydrolysis of raw and soluble starch. Food Res. Int., 42, 436-442.
    • (2009) Food Res. Int. , vol.42 , pp. 436-442
    • Gangadharan, D.1    Nampoothiri, K.M.2    Sivaramakrishnan, S.3    Pandey, A.4
  • 42
    • 58149242518 scopus 로고    scopus 로고
    • Production, purification and characterization of two extremely halotolerant, thermostable and alkali-stable α-amylases from Chromohalobacter sp. TVSP 101
    • Prakash, B., Vidyasagar, M., Madhukumar, M.S., Muaralikrishna, G., Sreeramalu, K., 2009. Production, purification and characterization of two extremely halotolerant, thermostable and alkali-stable α-amylases from Chromohalobacter sp. TVSP 101. Process Biochem. 44, 210-215.
    • (2009) Process Biochem. , vol.44 , pp. 210-215
    • Prakash, B.1    Vidyasagar, M.2    Madhukumar, M.S.3    Muaralikrishna, G.4    Sreeramalu, K.5
  • 43
    • 0026628849 scopus 로고
    • Haloalkaliphilic maltotriose-forming α-amylase from the archaebacterium Natronococcus sp. Strain Ah-36
    • Kobayashi, T., Kanai, H., Hayashi, T., Akiba, T., et al., 1992. Haloalkaliphilic maltotriose-forming α-amylase from the archaebacterium Natronococcus sp. Strain Ah-36. J. Bacteriol., 174, 3439-3444.
    • (1992) J. Bacteriol. , vol.174 , pp. 3439-3444
    • Kobayashi, T.1    Kanai, H.2    Hayashi, T.3    Akiba, T.4
  • 44
    • 0029119475 scopus 로고
    • Production and characterization of a maltotetraose-forming alkaline α-amylase from an alkalophilic Bacillus strain GM8901
    • Kim, T.U., Gu, B.G., Jeong, J.Y., Byun, S.M., Shin, Y.C., 1995. Production and characterization of a maltotetraose-forming alkaline α-amylase from an alkalophilic Bacillus strain GM8901. Appl. Environ. Microbiol., 61, 3105-3112.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3105-3112
    • Kim, T.U.1    Gu, B.G.2    Jeong, J.Y.3    Byun, S.M.4    Shin, Y.C.5
  • 45
    • 0031849201 scopus 로고    scopus 로고
    • Production and properties of a raw starch degrading amylase from the thermophilic and alkaliphilic Bacillus sp. TS-23
    • Lin, L.L., Chyau, C.C., Hsu, W.H., 1998. Production and properties of a raw starch degrading amylase from the thermophilic and alkaliphilic Bacillus sp. TS-23. Biotechnol. Appl. Biochem., 28, 61-68.
    • (1998) Biotechnol. Appl. Biochem. , vol.28 , pp. 61-68
    • Lin, L.L.1    Chyau, C.C.2    Hsu, W.H.3
  • 46
    • 84906260766 scopus 로고
    • Heat stable alkaline amylase from Bacillus Jpn. Kokai patent. 9.049, 584.
    • Ozaki, A., Tanaka, A., 1990. Heat stable alkaline amylase from Bacillus Jpn. Kokai patent. 9.049, 584.
    • (1990)
    • Ozaki, A.1    Tanaka, A.2
  • 47
    • 0343162263 scopus 로고
    • Extracellular alkaline amylase of alkalophilic bacteria
    • Boyer, E.W., Ingle, M.B., 1972. Extracellular alkaline amylase of alkalophilic bacteria. Agric. Biol. Chem., 36, 1819-1823.
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 1819-1823
    • Boyer, E.W.1    Ingle, M.B.2
  • 48
    • 0029560330 scopus 로고
    • Contribution of a disulfide bridge to the stability of 1,3-1,4-β-D-glucan 4-glucanohydrolase from Bacillus licheniformis
    • Pons, J., Planas, A., Enrique, Q., 1995. Contribution of a disulfide bridge to the stability of 1, 3-1, 4-β-D-glucan 4-glucanohydrolase from Bacillus licheniformis. Protein Eng., 8, 939-945.
    • (1995) Protein Eng. , vol.8 , pp. 939-945
    • Pons, J.1    Planas, A.2    Enrique, Q.3
  • 49
    • 0028943302 scopus 로고
    • Purification and properties of extracellular amylase from the hyperthermophilic archeon Thermococcus profundus DT5432
    • Chung, Y.C., Kobayashi, T., Kanai, H., Akiba, T., Kudo, T., 1995. Purification and properties of extracellular amylase from the hyperthermophilic archeon Thermococcus profundus DT5432. Appl. Environ. Microbiol., 61, 1502-1506.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1502-1506
    • Chung, Y.C.1    Kobayashi, T.2    Kanai, H.3    Akiba, T.4    Kudo, T.5
  • 50
    • 0030779216 scopus 로고    scopus 로고
    • Towards an understanding of starch granule structure and hydrolysis
    • Qates, C.G., 1997. Towards an understanding of starch granule structure and hydrolysis. Trends Food Sci. Technol., 8, 375-382.
    • (1997) Trends Food Sci. Technol. , vol.8 , pp. 375-382
    • Qates, C.G.1
  • 51
    • 0002809613 scopus 로고
    • Hydrolysis of starch granules by the amylase from Bacillus stearothermophilus NCA 26
    • Campus, B.G., Priest, F.G., Stark, J.R., 1992 Hydrolysis of starch granules by the amylase from Bacillus stearothermophilus NCA 26. Process Biochem., 27, 17-21.
    • (1992) Process Biochem. , vol.27 , pp. 17-21
    • Campus, B.G.1    Priest, F.G.2    Stark, J.R.3
  • 52
    • 0344223437 scopus 로고    scopus 로고
    • The evolution of starch-binding domain
    • Janecek, S., Sevcik, J., 1999. The evolution of starch-binding domain. FEBS Lett., 456, 119-125.
    • (1999) FEBS Lett. , vol.456 , pp. 119-125
    • Janecek, S.1    Sevcik, J.2
  • 54
    • 12644258001 scopus 로고    scopus 로고
    • The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251
    • Penninga, D., van der Veen, B.A., Knegtel, R.M.A., van Hijum, S.A.F.T., et al., 1996. The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251. Biol. Chem., 271, 32777-32784.
    • (1996) Biol. Chem. , vol.271 , pp. 32777-32784
    • Penninga, D.1    van der Veen, B.A.2    Knegtel, R.M.A.3    van Hijum, S.A.F.T.4


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