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
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
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
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
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
110. Fulekar MH (2010) Nanotechnology: importance and applications. K. International
Publication House, New Delhi
111. Watlington K (2005) Emerging nanotechnologies for site remediation and wastewater
treatment. US Environmental Protection Agency, Washington
112. Husain Q (2017) Nanomaterials as novel supports for the immobilization of amylolytic
enzymes and their applications. Biocatalysis 3:37–53
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
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
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
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
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
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
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
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
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
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
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
244
S. O. Hashim
maltooligosaccharide-producing amylases as antistaling agents for bread. J Agric Food Chem
46:779–782
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
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
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
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
110. Fulekar MH (2010) Nanotechnology: importance and applications. K. International
Publication House, New Delhi
111. Watlington K (2005) Emerging nanotechnologies for site remediation and wastewater
treatment. US Environmental Protection Agency, Washington
112. Husain Q (2017) Nanomaterials as novel supports for the immobilization of amylolytic
enzymes and their applications. Biocatalysis 3:37–53
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
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
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
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
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
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
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
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
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
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
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
244
S. O. Hashim