44. Kim TU, Gu BG, Jeong JY, Byun SM, Shin YC (1995) Purification and characterization of a
maltotetraose-forming alkaline (alpha)-amylase from an alkalophilic Bacillus Strain, GM8901.
Appl Environ Microbiol 61:3105–3112
45. Hayashi T, Akiba T, Horikoshi K (1988) Production and purification of new maltohexaoseforming amylases from alkalophilic Bacillus sp. H-167. Agric Biol Chem 52:443–448
46. Hayashi T, Akiba T, Horikoshi K (1988) Properties of new alkaline maltohexaose-forming
amylases. Appl Microbiol Biotechnol 28:281–285
47. Kanai R, Haga K, Akiba T, Yamane K, Harata K (2004) Biochemical and crystallographic
analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707. Biochemistry
43:14047–14056
48. Pan S, Ding N, Ren J, Gu Z, Li C, Hong Y, Cheng L, Holler TP, Li Z (2017)
Maltooligosaccharide-forming amylase: characteristics, preparation, and application.
Biotechnol Adv 35:619–632
49. Chegeni M, Hamaker B (2015) Induction of differentiation of small intestinal enterocyte cells
by maltooligosaccharides. FASEB J 29:596.14
50. Shieh WJ, Hedges AR (1996) Properties and applications of cyclodextrins. J Macromol Sci
Part A 33:673–683
51. Del Valle EMM (2004) Cyclodextrins and their uses: a review. Process Biochem
39:1033–1046
52. Astray G, Gonzalez-Barreiro C, Mejuto JC, Rial-Otero R, Simal-Gándara J (2009) A review
on the use of cyclodextrins in foods. Food Hydrocoll 23:1631–1640
53. Amiri S, Amiri S (2017) Cyclodextrin applications. Cyclodextrins. Wiley-Blackwell,
Chichester, pp 269–300
54. Biwer A, Antranikian G, Heinzle E (2002) Enzymatic production of cyclodextrins. Appl
Microbiol Biotechnol 59:609–617
55. Li Z, Wang M, Wang F, Gu Z, Du G, Wu J, Chen J (2007) γ-Cyclodextrin: a review
on enzymatic production and applications. Appl Microbiol Biotechnol 77:245–255
56. van der Veen BA, van Alebeek GJ, Uitdehaag JC, Dijkstra BW, Dijkhuizen L (2000) The three
transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus
circulans (strain 251) proceed via different kinetic mechanisms. Eur J Biochem 267:658–665
57. Janeček Š (1995) Close evolutionary relatedness among functionally distantly related members of the (α/β)8-barrel glycosyl hydrolases suggested by the similarity of their fifth conserved
sequence region. FEBS Lett 377:6–8
58. Ballschmiter M, Armbrecht M, Ivanova K, Antranikian G, Liebl W (2005) AmyA, an alphaamylase with beta-cyclodextrin-forming activity, and AmyB from the thermoalkaliphilic
organism Anaerobranca gottschalkii: two alpha-amylases adapted to their different cellular
localizations. Appl Environ Microbiol 71:3709–3715
59. Brumm PJ, Hebeda RE, Teague WM (1991) Purification and characterization of the commercialized, cloned bacillus megaterium α-amylase. Part I: purification and hydrolytic properties.
Starch-Stärke 43:315–319
60. Brumm PJ, Hebeda RE, Teague WM (1991) Purification and characterization of the commercialized, cloned Bacillus megaterium α-amylase. Part II: transferase properties. Starch-Stärke
43:319–323
61. Saha BC, Zeikus JG (1992) Cyclodextrin degrading enzymes. Starch-Stärke 44:312–315
62. Lin LL, Chyau CC, Hsu WH (1998) Production and properties of a raw-starch-degrading
amylase from the thermophilic and alkaliphilic Bacillus sp. TS-23. Biotechnol Appl Biochem
28(Pt 1):61–68
63. Horikoshi K (1999) Alkaliphiles: some applications of their products for biotechnology.
Microbiol Mol Biol Rev 63:735–750
64. Matzuzawa M, Kawano M, Nakamura N, Horikoshi K An improved method for the preparation of schardinger β-dextrin on an industrial scale by cyclodextrin glycosyl transferase of an
alkalophilic Bacillus Sp. (ATCC 21783). Starch-Stärke 27:410–413
Starch-Modifying Enzymes
241
maltotetraose-forming alkaline (alpha)-amylase from an alkalophilic Bacillus Strain, GM8901.
Appl Environ Microbiol 61:3105–3112
45. Hayashi T, Akiba T, Horikoshi K (1988) Production and purification of new maltohexaoseforming amylases from alkalophilic Bacillus sp. H-167. Agric Biol Chem 52:443–448
46. Hayashi T, Akiba T, Horikoshi K (1988) Properties of new alkaline maltohexaose-forming
amylases. Appl Microbiol Biotechnol 28:281–285
47. Kanai R, Haga K, Akiba T, Yamane K, Harata K (2004) Biochemical and crystallographic
analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707. Biochemistry
43:14047–14056
48. Pan S, Ding N, Ren J, Gu Z, Li C, Hong Y, Cheng L, Holler TP, Li Z (2017)
Maltooligosaccharide-forming amylase: characteristics, preparation, and application.
Biotechnol Adv 35:619–632
49. Chegeni M, Hamaker B (2015) Induction of differentiation of small intestinal enterocyte cells
by maltooligosaccharides. FASEB J 29:596.14
50. Shieh WJ, Hedges AR (1996) Properties and applications of cyclodextrins. J Macromol Sci
Part A 33:673–683
51. Del Valle EMM (2004) Cyclodextrins and their uses: a review. Process Biochem
39:1033–1046
52. Astray G, Gonzalez-Barreiro C, Mejuto JC, Rial-Otero R, Simal-Gándara J (2009) A review
on the use of cyclodextrins in foods. Food Hydrocoll 23:1631–1640
53. Amiri S, Amiri S (2017) Cyclodextrin applications. Cyclodextrins. Wiley-Blackwell,
Chichester, pp 269–300
54. Biwer A, Antranikian G, Heinzle E (2002) Enzymatic production of cyclodextrins. Appl
Microbiol Biotechnol 59:609–617
55. Li Z, Wang M, Wang F, Gu Z, Du G, Wu J, Chen J (2007) γ-Cyclodextrin: a review
on enzymatic production and applications. Appl Microbiol Biotechnol 77:245–255
56. van der Veen BA, van Alebeek GJ, Uitdehaag JC, Dijkstra BW, Dijkhuizen L (2000) The three
transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus
circulans (strain 251) proceed via different kinetic mechanisms. Eur J Biochem 267:658–665
57. Janeček Š (1995) Close evolutionary relatedness among functionally distantly related members of the (α/β)8-barrel glycosyl hydrolases suggested by the similarity of their fifth conserved
sequence region. FEBS Lett 377:6–8
58. Ballschmiter M, Armbrecht M, Ivanova K, Antranikian G, Liebl W (2005) AmyA, an alphaamylase with beta-cyclodextrin-forming activity, and AmyB from the thermoalkaliphilic
organism Anaerobranca gottschalkii: two alpha-amylases adapted to their different cellular
localizations. Appl Environ Microbiol 71:3709–3715
59. Brumm PJ, Hebeda RE, Teague WM (1991) Purification and characterization of the commercialized, cloned bacillus megaterium α-amylase. Part I: purification and hydrolytic properties.
Starch-Stärke 43:315–319
60. Brumm PJ, Hebeda RE, Teague WM (1991) Purification and characterization of the commercialized, cloned Bacillus megaterium α-amylase. Part II: transferase properties. Starch-Stärke
43:319–323
61. Saha BC, Zeikus JG (1992) Cyclodextrin degrading enzymes. Starch-Stärke 44:312–315
62. Lin LL, Chyau CC, Hsu WH (1998) Production and properties of a raw-starch-degrading
amylase from the thermophilic and alkaliphilic Bacillus sp. TS-23. Biotechnol Appl Biochem
28(Pt 1):61–68
63. Horikoshi K (1999) Alkaliphiles: some applications of their products for biotechnology.
Microbiol Mol Biol Rev 63:735–750
64. Matzuzawa M, Kawano M, Nakamura N, Horikoshi K An improved method for the preparation of schardinger β-dextrin on an industrial scale by cyclodextrin glycosyl transferase of an
alkalophilic Bacillus Sp. (ATCC 21783). Starch-Stärke 27:410–413
Starch-Modifying Enzymes
241