Skip to main content

Starch-Modifying Enzymes

  • Chapter
  • First Online:
Alkaliphiles in Biotechnology

Part of the book series: Advances in Biochemical Engineering/Biotechnology ((ABE,volume 172))

Abstract

Starch is a carbohydrate polymer found abundantly on earth. It is synthesized in plants as a short-term storage compound for respiration in the leaves and for long-term storage in the tubers, seeds and roots of plants. A wide variety of enzymes modify or convert starch into various products. The classes of enzymes that act on starch include endoamylases, exoamylases, debranching enzymes and transferases. Starch-modifying enzymes of microbial origin are utilized in a wide variety of industrial applications. Alkaline-active amylases are diverse in terms of optimum reaction conditions, substrate and product specificity. Amylases that are active at lower temperatures and alkaline conditions are most suited for detergent formulation. Other notable starch-modifying enzymes from alkaliphiles include maltooligosaccharide-forming amylases and cyclodextrin glycosyltransferases (CGTases), which produce a variety of maltooligosaccharides and cyclodextrins, respectively. Such compounds are used in the food, fine chemical, pharmaceutical and cosmetic industries, among others. Alkaline-active amylases are also applicable in the paper, textile and leather industries and also in bioremediation and alkaline waste water treatment. Their application in these fields is further enhanced through stabilization and improving their specificity and catalytic action by employing nanotechnology and genetic engineering.

Graphical Abstract *Alkaline alpha-amylase AmyK from Bacillus sp. KSM-1378. Shirai T, Igarashi K, Ozawa T, Hagihara H, Kobayashi T, Ozaki K, Ito S (2007) Proteins 66:600–610. Source: Protein Data Bank in Europe (PDBe)

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 299.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 379.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 379.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Abbreviations

AKD:

Alkylketene dimer

ASA:

Alkenylsuccinic anhydride

BAA:

Bacillus amyloliquefaciens amylase

CDs:

Cyclodextrins

CGTases:

Cyclodextrin glycosyltransferases

DDM:

Dodecyl-β-d-maltoside

DDMO:

Dodecyl-β-d-maltooctaoside

DE:

Dextrose equivalent

DP:

Degree of polymerization

EC:

Enzyme Commission

EDTA:

Ethylenediaminetetraacetic acid

EGTA:

Ethylene glycol tetraacetic acid

kDa:

Kilodalton

MNPs:

Magnetic nanoparticles

SEN:

Single-enzyme nanoparticle

References

  1. Singh J, Kaur L, McCarthy OJ (2007) Factors influencing the physico-chemical, morphological, thermal and rheological properties of some chemically modified starches for food applications – a review. Food Hydrocoll 21(1):1–22

    Article  CAS  Google Scholar 

  2. van der Maarel MJEC, van der Veen B, Uitdehaag JCM, Leemhuis H, Dijkhuizen L (2002) Properties and applications of starch-converting enzymes of the alpha-amylase family. J Biotechnol 94:137–155

    Article  PubMed  Google Scholar 

  3. Janecek S (1997) alpha-Amylase family: molecular biology and evolution. Prog Biophys Mol Biol 67:67–97

    Article  CAS  PubMed  Google Scholar 

  4. Janecek S (2000) Amylolytic enzymes: their specificities, origins and properties. Biologia-Bratislava 55:605–615

    Google Scholar 

  5. Kuriki T, Imanaka T (1999) The concept of the alpha-amylase family: structural similarity and common catalytic mechanism. J Biosci Bioeng 87:557–565

    Article  CAS  PubMed  Google Scholar 

  6. Vihinen M, Mäntsälä P (1989) Microbial amylolytic enzymes. Crit Rev Biochem Mol Biol 24:329–418

    Article  CAS  PubMed  Google Scholar 

  7. Rajagopalan G, Krishnan C (2008) Alpha-amylase production from catabolite derepressed Bacillus subtilis KCC103 utilizing sugarcane bagasse hydrolysate. Bioresour Technol 99:3044–3050

    Article  CAS  PubMed  Google Scholar 

  8. Reddy NS, Nimmagadda A, Sambasiva Rao KRS (2003) An overview of the microbial α-amylase family. Afr J Biotechnol 2:645–648

    Article  CAS  Google Scholar 

  9. Hmidet N, El-Hadj Ali N, Haddar A, Kanoun S, Alya S-K, Nasri M (2009) Alkaline proteases and thermostable α-amylase co-produced by Bacillus licheniformis NH1: characterization and potential application as detergent additive. Biochem Eng J 47:71–79

    Article  CAS  Google Scholar 

  10. Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B (2003) Microbial α-amylases: a biotechnological perspective. Process Biochem 38:1599–1616

    Article  CAS  Google Scholar 

  11. Pandey A, Nigam P, Soccol CR, Soccol VT, Singh D, Mohan R (2000) Advances in microbial amylases. Biotechnol Appl Biochem 31(Pt 2):135–152

    Article  CAS  PubMed  Google Scholar 

  12. Kandra L (2003) α-Amylases of medical and industrial importance. J Mol Struct (THEOCHEM) 666–667:487–498

    Article  CAS  Google Scholar 

  13. Kirk O, Borchert TV, Fuglsang CC (2002) Industrial enzyme applications. Curr Opin Biotechnol 13:345–351

    Article  CAS  PubMed  Google Scholar 

  14. de Souza PM, de Oliveira Magalhães P (2010) Application of microbial α-amylase in industry – a review. Braz J Microbiol 41:850–861

    Article  PubMed  PubMed Central  Google Scholar 

  15. Mobini-Dehkordi M, Javan FA (2012) Application of alpha-amylase in biotechnology. J Biol Today’s World 1:15–20

    Google Scholar 

  16. Vaidya S, Srivastava PK, Rathore DP, Pandey AK (2015) Amylases: a prospective enzyme in the field of biotechnology, vol 41, pp 1–18

    Google Scholar 

  17. Horikoshi K (1971) Production of alkaline enzymes by alkalophilic microorganisms part II. Alkaline amylase produced by Bacillus No. A-40-2. Agric Biol Chem 35:1783–1791

    Article  CAS  Google Scholar 

  18. Yamamoto M, Tanaka Y, Horikoshi K (1972) Alkaline amylases of alkalophilic bacteria. Agric Biol Chem 36:1819–1823

    Article  CAS  Google Scholar 

  19. Mitidieri S, Souza Martinelli AH, Schrank A, Vainstein MH (2006) Enzymatic detergent formulation containing amylase from Aspergillus niger: a comparative study with commercial detergent formulations. Bioresour Technol 97:1217–1224

    Article  CAS  PubMed  Google Scholar 

  20. Mukherjee AK, Borah M, Rai SK (2009) To study the influence of different components of fermentable substrates on induction of extracellular α-amylase synthesis by Bacillus subtilis DM-03 in solid-state fermentation and exploration of feasibility for inclusion of α-amylase in laundry detergent formulations. Biochem Eng J 43:149–156

    Article  CAS  Google Scholar 

  21. Olsen HS, Falholt P (1998) The role of enzymes in modern detergency. J Surfactant Deterg 1:555–567

    Article  CAS  Google Scholar 

  22. Chi M-C, Chen Y-H, Wu T-J, Lo H-F, Lin L-L (2010) Engineering of a truncated α-amylase of Bacillus sp. strain TS-23 for the simultaneous improvement of thermal and oxidative stabilities. J Biosci Bioeng 109:531–538

    Article  CAS  PubMed  Google Scholar 

  23. Vallee BL, Stein EA, Sumerwell WN, Fischer EH (1959) Metal content of alpha-amylases of various origins. J Biol Chem 234:2901–2905

    Article  CAS  PubMed  Google Scholar 

  24. Janeček Š, Baláž Š (1992) α-Amylases and approaches leading to their enhanced stability. FEBS Lett 304:1–3

    Article  PubMed  Google Scholar 

  25. Hagihara H, Igarashi K, Hayashi Y, Endo K, Ikawa-Kitayama K, Ozaki K, Kawai S, Ito S (2001) Novel α-amylase that is highly resistant to chelating reagents and chemical oxidants from the alkaliphilic Bacillus isolate KSM-K38. Appl Environ Microbiol 67:1744–1750

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  26. Dahiya P, Rathi P (2015) Characterization and application of alkaline α-amylase from Bacillus licheniformis MTCC1483 as a detergent additive. Int Food Res J 22:1293–1297

    CAS  Google Scholar 

  27. Arikan B (2008) Highly thermostable, thermophilic, alkaline, SDS and chelator resistant amylase from a thermophilic Bacillus sp. isolate A3-15. Bioresour Technol 99:3071–3076

    Article  CAS  PubMed  Google Scholar 

  28. Saxena RK, Dutt K, Agarwal L, Nayyar P (2007) A highly thermostable and alkaline amylase from a Bacillus sp. PN5. Bioresour Technol 98:260–265

    Article  CAS  PubMed  Google Scholar 

  29. Burhan A, Coral G, Colak O, Aygan A, Gulnaz O (2003) Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. Isolate ANT-6. Process Biochem 38:1397–1403

    Article  CAS  Google Scholar 

  30. 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

    Article  CAS  Google Scholar 

  31. Igarashi K, Hatada Y, Hagihara H, Saeki K, Takaiwa M, Uemura T, Ara K, Ozaki K, Kawai S, Kobayashi T, Ito S (1998) Enzymatic properties of a novel liquefying α-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences. Appl Environ Microbiol 64:3282–3289

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  32. Bernhardsdotter ECMJ, Ng JD, Garriott OK, Pusey ML (2005) Enzymic properties of an alkaline chelator-resistant α-amylase from an alkaliphilic Bacillus sp. isolate L1711. Process Biochem 40:2401–2408

    Article  CAS  Google Scholar 

  33. Ito S, Kobayashi T, Ara K, Ozaki K, Kawai S, Hatada Y (1998) Alkaline detergent enzymes from alkaliphiles: enzymatic properties, genetics, and structures. Extremophiles 2:185–190

    Article  CAS  PubMed  Google Scholar 

  34. Nakamura N, Watanabe K, Horikoshi K (1975) Purification and some properties of alkaline pullulanase from a strain of Bacillus No. 202-1, an alkalophilic microorganism. Biochim Biophys Acta 397:188–193

    Article  CAS  PubMed  Google Scholar 

  35. Kim C-H, Choi H-I, Lee D-S (1993) Pullulanases of alkaline and broad pH range from a newly isolated alkalophilic Bacillus sp. S-1 and a Micrococcus sp. Y-1. J Ind Microbiol 12:48–57

    Article  CAS  Google Scholar 

  36. Kim C-H, Choi H-I, Lee D-S (1993) Purification and biochemical properties of an alkaline pullulanase from Alkalophilic Bacillus sp. S-l. Biosci Biotechnol Biochem 57:1632–1637

    Article  CAS  PubMed  Google Scholar 

  37. Ara K, Igarashi K, Saeki K, Kawai S, Ito S (1992) Purification and some properties of an alkaline pullulanase from alkalophilic Bacillus sp. KSM-1876. Biosci Biotechnol Biochem 56:62–65

    Article  CAS  Google Scholar 

  38. Ara K, Saeki K, Igarashi K, Takaiwa M, Uemura T, Hagihara H, Kawai S, Ito S (1995) Purification and characterization of an alkaline amylopullulanase with both alpha-1,4 and alpha-1,6 hydrolytic activity from alkalophilic Bacillus sp. KSM-1378. Biochim Biophys Acta 1243:315–324

    Article  PubMed  Google Scholar 

  39. Igarashi K, Ara K, Saeki K, Ozaki K, Kawai S, Ito S (1992) Nucleotide sequence of the gene that encodes a neopullulanase from an alkalophilic Bacillus. Biosci Biotechnol Biochem 56:514–516

    Article  CAS  PubMed  Google Scholar 

  40. Ara K, Saeki K, Ito S (1993) Purification and characterization of an alkaline isoamylase from an alkalophilic strain of Bacillus. J Gen Microbiol 139:781–786

    Article  CAS  Google Scholar 

  41. Bessler C, Schmitt J, Maurer K-H, Schmid RD (2003) Directed evolution of a bacterial α-amylase: toward enhanced pH-performance and higher specific activity. Protein Sci 12:2141–2149

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  42. Nakano M, Chaen H, Sugimoto T, Miyake T (2001) Maltohexaose and maltoheptaose-forming amylase, and its preparation and uses. Patent no. US6242224B1

    Google Scholar 

  43. Hashim SO, Delgado OD, Martínez MA, Kaul R-H, Mulaa FJ, Mattiasson B (2005) Alkaline active maltohexaose-forming α-amylase from Bacillus halodurans LBK 34. Enzyme Microb Technol 36:139–146

    Article  CAS  Google Scholar 

  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

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  45. Hayashi T, Akiba T, Horikoshi K (1988) Production and purification of new maltohexaose-forming amylases from alkalophilic Bacillus sp. H-167. Agric Biol Chem 52:443–448

    CAS  Google Scholar 

  46. Hayashi T, Akiba T, Horikoshi K (1988) Properties of new alkaline maltohexaose-forming amylases. Appl Microbiol Biotechnol 28:281–285

    Article  CAS  Google Scholar 

  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

    Article  CAS  PubMed  Google Scholar 

  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

    Article  CAS  PubMed  Google Scholar 

  49. Chegeni M, Hamaker B (2015) Induction of differentiation of small intestinal enterocyte cells by maltooligosaccharides. FASEB J 29:596.14

    Article  Google Scholar 

  50. Shieh WJ, Hedges AR (1996) Properties and applications of cyclodextrins. J Macromol Sci Part A 33:673–683

    Article  Google Scholar 

  51. Del Valle EMM (2004) Cyclodextrins and their uses: a review. Process Biochem 39:1033–1046

    Article  CAS  Google Scholar 

  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

    Article  CAS  Google Scholar 

  53. Amiri S, Amiri S (2017) Cyclodextrin applications. Cyclodextrins. Wiley-Blackwell, Chichester, pp 269–300

    Chapter  Google Scholar 

  54. Biwer A, Antranikian G, Heinzle E (2002) Enzymatic production of cyclodextrins. Appl Microbiol Biotechnol 59:609–617

    Article  CAS  PubMed  Google Scholar 

  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

    Article  CAS  PubMed  Google Scholar 

  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

    Article  PubMed  Google Scholar 

  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

    Article  PubMed  Google Scholar 

  58. Ballschmiter M, Armbrecht M, Ivanova K, Antranikian G, Liebl W (2005) AmyA, an alpha-amylase 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

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  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

    Article  CAS  Google Scholar 

  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

    Article  CAS  Google Scholar 

  61. Saha BC, Zeikus JG (1992) Cyclodextrin degrading enzymes. Starch-Stärke 44:312–315

    Article  CAS  Google Scholar 

  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

    CAS  PubMed  Google Scholar 

  63. Horikoshi K (1999) Alkaliphiles: some applications of their products for biotechnology. Microbiol Mol Biol Rev 63:735–750

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  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

    Google Scholar 

  65. Nakamura N, Horikoshi K (1976) Purification and properties of cyclodextrin glycosyltransferase of an alkalophilic Bacillus sp. Agric Biol Chem 40:935–941

    Article  CAS  Google Scholar 

  66. Kim MH, Sohn CB, Oh TK (1998) Cloning and sequencing of a cyclodextrin glycosyltransferase gene from Brevibacillus brevis CD162 and its expression in Escherichia coli. FEMS Microbiol Lett 164:411–418

    Article  CAS  PubMed  Google Scholar 

  67. Atanasova N, Kitayska T, Bojadjieva I, Yankov D, Tonkova A (2011) A novel cyclodextrin glucanotransferase from alkaliphilic Bacillus pseudalcaliphilus 20RF: purification and properties. Process Biochem 46:116–122

    Article  CAS  Google Scholar 

  68. Thiemann V, Dönges C, Prowe SG, Sterner R, Antranikian G (2004) Characterisation of a thermoalkali-stable cyclodextrin glycosyltransferase from the anaerobic thermoalkaliphilic bacterium Anaerobranca gottschalkii. Arch Microbiol 182:226–235

    Article  CAS  PubMed  Google Scholar 

  69. Cao X, Jin Z, Wang X, Chen F (2005) A novel cyclodextrin glycosyltransferase from an alkalophilic Bacillus species: purification and characterization. Food Res Int 38:309–314

    Article  CAS  Google Scholar 

  70. Moriwaki C, Ferreira LR, Rodella JRT, Matioli G (2009) A novel cyclodextrin glycosyltransferase from Bacillus sphaericus strain 41: production, characterization and catalytic properties. Biochem Eng J 48:124–131

    Article  CAS  Google Scholar 

  71. Vassileva A, Atanasova N, Ivanova V, Dhulster P, Tonkova A (2007) Characterisation of cyclodextrin glucanotransferase from Bacillus circulans ATCC 21783 in terms of cyclodextrin production. Ann Microbiol 57:609–615

    Article  CAS  Google Scholar 

  72. Yim DG, Sato HH, Park YH, Park YK (1997) Production of cyclodextrin from starch by cyclodextrin glycosyltransferase from Bacillus firmus and characterization of purified enzyme. J Ind Microbiol Biotechnol 18:402–405

    Article  CAS  Google Scholar 

  73. Hirano K, Ishihara T, Ogasawara S, Maeda H, Abe K, Nakajima T, Yamagata Y (2006) Molecular cloning and characterization of a novel γ-CGTase from alkalophilic Bacillus sp. Appl Microbiol Biotechnol 70:193–201

    Article  CAS  PubMed  Google Scholar 

  74. Martins RF, Hatti-Kaul R (2002) A new cyclodextrin glycosyltransferase from an alkaliphilic Bacillus agaradhaerens isolate: purification and characterisation. Enzyme Microb Technol 30:116–124

    Article  CAS  Google Scholar 

  75. Penninga D, Strokopytov B, Rozeboom HJ, Lawson CL, Dijkstra BW, Bergsma J, Dijkhuizen L (1995) Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity. Biochemistry 34:3368–3376

    Article  CAS  PubMed  Google Scholar 

  76. Moriwaki C, Costa GL, Pazzetto R, Zanin GM, Moraes FF, Portilho M, Matioli G (2007) Production and characterization of a new cyclodextrin glycosyltransferase from Bacillus firmus isolated from Brazilian soil. Process Biochem 42:1384–1390

    Article  CAS  Google Scholar 

  77. Ibrahim ASS, Al-Salamah AA, El-Tayeb MA, El-Badawi YB, Antranikian G (2012) A Novel Cyclodextrin Glycosyltransferase from Alkaliphilic Amphibacillus sp. NPST-10: Purification and Properties. Int J Mol Sci 13:10505–10522

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  78. Alves-Prado HF, AAJ Carneiro, FC Pavezzi, E Gomes, M Boscolo, CML Franco, R da Silva (2007) Production of cyclodextrins by CGTase from Bacillus clausii using different starches as substrates. In: Biotechnology for fuels and chemicals, Humana Press, Totowa, NJ, pp 123–133

    Google Scholar 

  79. Mori S, Hirose S, Oya T, Kitahata S (1994) Purification and properties of cyclodextrin glucanotransferase from Brevibacterium sp. No. 9605. Biosci Biotechnol Biochem 58:1968–1972

    Article  CAS  Google Scholar 

  80. Takada M, Nakagawa Y, Yamamoto M (2003) Biochemical and genetic analyses of a novel γ-cyclodextrin glucanotransferase from an Alkalophilic Bacillus clarkii 7364. J Biochem 133:317–324

    Article  CAS  PubMed  Google Scholar 

  81. Takada M, Ide T, Yamamoto T, Unno T, Watanabe Y, Sone H, Yamamoto M (2003) Novel cyclodextrin glucanotransferase, process for producing the same and process for producing cyclodextrin by using this enzyme. Patent no. US20030194796A1

    Google Scholar 

  82. Matioli G, Zanin GM, de Moraes FF (2000) Enhancement of selectivity for producing γ-cyclodextrin. In: Twenty-first symposium on biotechnology for fuels and chemicals, Humana Press, Totowa, NJ, pp 955–962

    Google Scholar 

  83. van der Veen BA, Uitdehaag JC, Dijkstra BW, Dijkhuizen L (2000) Engineering of cyclodextrin glycosyltransferase reaction and product specificity. Biochim Biophys Acta 1543:336–360

    Article  PubMed  Google Scholar 

  84. Parsiegla G, Schmidt AK, Schulz GE Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the γ-cyclodextrin production. Eur J Biochem 255:710–717

    Google Scholar 

  85. Lee K-W, Shin H-D, Lee Y-H (2003) Catalytic function and affinity purification of site-directed mutant β-cyclodextrin glucanotransferase from alkalophilic Bacillus firmus var. alkalophilus. J Mol Catal B: Enzym 26:157–165

    Article  CAS  Google Scholar 

  86. Wang L, Duan X, Wu J (2016) Enhancing the α-cyclodextrin specificity of cyclodextrin glycosyltransferase from Paenibacillus macerans by mutagenesis masking subsite -7. Appl Environ Microbiol 82:2247–2255

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  87. Feng T, Zhuang H, Ran Y (2011) The application of cyclodextrin glycosyltransferase in biological science. J Bioequiv Bioavailab 3:202–206

    CAS  Google Scholar 

  88. Taira H, Nagase H, Endo T, Ueda H (2006) Isolation, purification and characterization of large-ring cyclodextrins (CD36–CD39). J Incl Phenom Macrocycl Chem 56:23–28

    Article  CAS  Google Scholar 

  89. Zheng M, Endo T, Zimmermann W (2002) Synthesis of large-ring cyclodextrins by cyclodextrin glucanotransferases from bacterial isolates. J Incl Phenom 44:387–390

    Article  CAS  Google Scholar 

  90. Svensson D, Ulvenlund S, Adlercreutz P (2009) Efficient synthesis of a long carbohydrate chain alkyl glycoside catalyzed by cyclodextrin glycosyltransferase (CGTase). Biotechnol Bioeng 104:854–861

    Article  CAS  PubMed  Google Scholar 

  91. Svensson D, Adlercreutz P (2011) Immobilisation of CGTase for continuous production of long-carbohydrate-chain alkyl glycosides Control of product distribution by flow rate adjustment. J Mol Catal B: Enzym 69:147–153

    Article  CAS  Google Scholar 

  92. Svensson D, Adlercreutz P (2011) Characterisation of a glycosylated alkyl polyglycoside produced by a cyclodextrin glycosyltransferase by HPLC-ELSD and -MS. J Chromatogr B 879:1857–1860

    Article  CAS  Google Scholar 

  93. Simair AA, Khushk I, Qureshi AS, Bhutto MA, Chaudhry HA, Ansari KA, Lu C (2017) Amylase production from thermophilic Bacillus sp. BCC 021-50 isolated from a marine environment. Fermentation 3:1–12

    Article  CAS  Google Scholar 

  94. Hamilton LM, Kelly CT, Fogarty WM (1999) Production and properties of the raw starch-digesting α-amylase of Bacillus sp. IMD 435. Process Biochem 35:27–31

    Article  CAS  Google Scholar 

  95. Asgher M, Javaid Asad M, Rahman S, Legge R (2007) A thermostable α-amylase from a moderately thermophilic Bacillus subtilis strain for starch processing. J Food Eng 79:950–955

    Article  CAS  Google Scholar 

  96. Asha R, Nyonzima FN, Sunil SM (2013) Purification and properties of pullulanase from Bacillus halodurans. Int Res J Biol Sci 2:35–43

    Google Scholar 

  97. Spendler T, Jorgensen OB (1997) Use of a branching enzyme in baking. Patent no. PCT/DK1997/000202

    Google Scholar 

  98. Cole MS (1982) Antistaling baking composition. Patent no. US05862653

    Google Scholar 

  99. Stefanis VAD, Turner EW (1981) Modified enzyme system to inhibit bread firming method for preparing same and use of same in bread and other bakery products. Patent no. US4299848A

    Google Scholar 

  100. Würsch P, Gumy D (1994) Inhibition of amylopectin retrogradation by partial beta-amylolysis. Carbohydr Res 256:129–137

    Article  PubMed  Google Scholar 

  101. Olesen T (1991) Antistaling process and agent. Patent no. PCT/DK1990/000244

    Google Scholar 

  102. Okada S, Kitahata S, Yoshikawa S, Sugimoto T, Sugimoto K (1984) Process for the production of branching enzyme, and a method for improving the qualities of food products therewith. Patent no. US4454161A

    Google Scholar 

  103. Carroll JO, Boyce COL, Wong TM, Starace CA (1987) Bread antistaling method. Patent no. US06760877

    Google Scholar 

  104. Vidal FD, Gerrity AB (1979) Antistaling agent for bakery products. Patent no. US05788193

    Google Scholar 

  105. Min B-C, Yoon S-H, Kim J-W, Lee Y-W, Kim Y-B, Park KH (1998) Cloning of novel maltooligosaccharide-producing amylases as antistaling agents for bread. J Agric Food Chem 46:779–782

    Article  CAS  PubMed  Google Scholar 

  106. Auh JH, Lee SY, Seung SY, Son HJ, Lee JW, Lee SI, Kim YB, Park KH (2005) A novel maltopentaose producing amylase as a bread antistaling agent. Food Sci Biotech 14:681–684

    CAS  Google Scholar 

  107. Hubbe MA (2004) Acidic and alkaline sizing for printing, writing and drawing papers. In: The Book and Paper Group Annual, American Institute for Conservation, Washington, pp 139–151

    Google Scholar 

  108. Lee SP, Morikawa M, Takagi M, Imanaka T (1994) Cloning of the aapT gene and characterization of its product, alpha-amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601. Appl Environ Microbiol 60:3764–3773

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  109. Kumar R, Sharma A, Dhall P, Kulshreshtha NM, Kumar A (2011) Neutralization of alkaline waste waters using a blend of microorganisms. Int J Biotechnol Bioeng 5:224–227

    Google Scholar 

  110. Fulekar MH (2010) Nanotechnology: importance and applications. K. International Publication House, New Delhi

    Google Scholar 

  111. Watlington K (2005) Emerging nanotechnologies for site remediation and wastewater treatment. US Environmental Protection Agency, Washington

    Google Scholar 

  112. Husain Q (2017) Nanomaterials as novel supports for the immobilization of amylolytic enzymes and their applications. Biocatalysis 3:37–53

    Article  Google Scholar 

  113. Mukherjee AK, Kumar TS, Rai SK, Roy JK (2010) Statistical optimization of Bacillus alcalophilus α-amylase immobilization on iron-oxide magnetic nanoparticles. Biotechnol Bioproc Eng 15:984–992

    Article  CAS  Google Scholar 

  114. Pandi A, Ramalingam S, Rao JR, Kamini NR, Gowthaman MK (2016) Inexpensive α-amylase production and application for fiber splitting in leather processing. RSC Adv 6:33170–33176

    Article  CAS  Google Scholar 

  115. Gupta RK, Prasad D, Sathesh J, Naidu RB, Kamini NR, Palanivel S, Gowthaman MK (2012) Scale-up of an alkaline protease from Bacillus pumilus MTCC 7514 utilizing fish meal as a sole source of nutrients. J Microbiol Biotechnol 22:1230–1236

    Article  CAS  PubMed  Google Scholar 

  116. Saran S, Mahajan RV, Kaushik R, Isar J, Saxena RK (2013) Enzyme mediated beam house operations of leather industry: a needed step towards greener technology. J Clean Prod 54:315–322

    Article  CAS  Google Scholar 

  117. Murakami S, Nagasaki K, Nishimoto H, Shigematu R, Umesaki J, Takenaka S, Kaulpiboon J, Prousoontorn M, Limpaseni T, Pongsawasdi P, Aoki K (2008) Purification and characterization of five alkaline, thermotolerant, and maltotetraose-producing α-amylases from Bacillus halodurans MS-2-5, and production of recombinant enzymes in Escherichia coli. Enzyme Microb Technol 43:321–328

    Article  CAS  Google Scholar 

  118. Ma Y, Yang H, Chen X, Sun B, Du G, Zhou Z, Song J, Fan Y, Shen W (2015) Significantly improving the yield of recombinant proteins in Bacillus subtilis by a novel powerful mutagenesis tool (ARTP): alkaline alpha-amylase as a case study. Protein Expr Purif 114:82–88

    Article  CAS  PubMed  Google Scholar 

  119. Yang H, Liu L, Wang M, Li J, Wang NS, Du G, Chen J (2012) Structure-based engineering of methionine residues in the catalytic cores of alkaline amylase from Alkalimonas amylolytica for improved oxidative stability. Appl Environ Microbiol 78:7519–7526

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  120. Yang H, Liu L, Shin H, Chen RR, Li J, Du G, Chen J (2013) Integrating terminal truncation and oligopeptide fusion for a novel protein engineering strategy to improve specific activity and catalytic efficiency: alkaline α-amylase as a case study. Appl Environ Microbiol 79:6429–6438

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  121. Tigue MAM, Kelly CT, Doyle EM, Fogarty WM (1995) The alkaline amylase of the alkalophilic Bacillus sp. IMD 370. Enzyme Microb Technol 17:570–573

    Article  Google Scholar 

  122. Duedahl-Olesen L, Kragh KM, Zimmermann W (2000) Purification and characterisation of a malto-oligosaccharide-forming amylase active at high pH from Bacillus clausii BT-21. Carbohydr Res 329:97–107

    Article  CAS  PubMed  Google Scholar 

  123. Bezbaruah RL, Gogoi BK, Pillai KR, Nigam JN (1991) Amylase production by three Bacillus strains active at alkaline pH. J Basic Microbiol 31:13–20

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Suhaila Omar Hashim .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2019 Springer Nature Switzerland AG

About this chapter

Check for updates. Verify currency and authenticity via CrossMark

Cite this chapter

Hashim, S.O. (2019). Starch-Modifying Enzymes. In: Mamo, G., Mattiasson, B. (eds) Alkaliphiles in Biotechnology. Advances in Biochemical Engineering/Biotechnology, vol 172. Springer, Cham. https://doi.org/10.1007/10_2019_91

Download citation

Publish with us

Policies and ethics