α-Amylase from Bacillus amyloliquefaciens

Product Description

α-Amylase from Bacillus amyloliquefaciens
Catalog number: B2011000
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 5 g
Molecular Weight or Concentration: na
Supplied as: Powder
Applications: molecular tool for various biochemical studies
Storage: -20C
Keywords: Bacillus amyloliquefaciens α-Amylase
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References:
1: Jujjavarapu SE, Dhagat S. Evolutionary Trends in Industrial Production of α-amylase Recent Pat Biotechnol. 2019;13(1):4-18.
2: Du R, Zhao F, Qiao X, Song Q, Ye G, Wang Y, Wang B, Han Y, Zhou Z. Optimization and partial characterization of ca-independent α-amylase from Bacillus amyloliquefaciens BH1 Prep Biochem Biotechnol. 2018;48(8):768-774.
3: EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Silano V, Barat Baviera JM, Bolognesi C, Cocconcelli PS, Crebelli R, Gott DM, Grob K, Lampi E, Mortensen A, Rivière G, Steffensen IL, Tlustos C, van Loveren H, Vernis L, Zorn H, Glandorf B, Herman L, Andryszkiewicz M, Arcella D, Gomes A, Liu Y, Chesson A. Safety evaluation of the food enzyme α-amylase from Bacillus amyloliquefaciens strain BANSC EFSA J. 2020 Jan 20;18(1):e05976.
4: Tang S, Xu T, Peng J, Zhou K, Zhu Y, Zhou W, Cheng H, Zhou H. Overexpression of an endogenous raw starch digesting mesophilic α-amylase gene in Bacillus amyloliquefaciens Z3 by in vitro methylation protocol J Sci Food Agric. 2020 May;100(7):3013-3023.
5: EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Silano V, Barat Baviera JM, Bolognesi C, Cocconcelli PS, Crebelli R, Gott DM, Grob K, Lambré C, Lampi E, Mengelers M, Mortensen A, Rivière G, Steffensen IL, Tlustos C, Van Loveren H, Vernis L, Zorn H, Herman L, Gomes A, Andryszkiewicz M, Kovalkovicova N, Liu Y, Chesson A. Safety evaluation of the food enzyme α-amylase from the genetically modified Bacillus amyloliquefaciens strain DP-Czb53 EFSA J. 2020 Oct 28;18(10):e06185.
6: Palva I. Molecular cloning of alpha-amylase gene from Bacillus amyloliquefaciens and its expression in B. subtilis Gene. 1982 Jul-Aug;19(1):81-7.
7: EFSA Panel on Additives and Products or Substances used in Animal Feed (FEEDAP), Rychen G, Aquilina G, Azimonti G, Bampidis V, Bastos ML, Bories G, Chesson A, Cocconcelli PS, Flachowsky G, Gropp J, Kolar B, Kouba M, López Puente S, López-Alonso M, Mantovani A, Mayo B, Ramos F, Saarela M, Villa RE, Wallace RJ, Wester P, Brantom P, Dierick NA, Aguilera J, Anguita M. Safety and efficacy of alpha-amylase from Bacillus amyloliquefaciens DSM 9553, Bacillus amyloliquefaciens NCIMB 30251, Aspergillus oryzae CBS 585.94 and Aspergillus oryzae ATTC SD-5374, endo-1,4-beta-glucanase from Trichoderma reesei ATCC PTA-10001, Trichoderma reesei ATCC SD-6331 and Aspergillus niger CBS 120604, endo-1,4-beta-xylanase from Trichoderma koningii MUCL 39203 and Trichoderma citrinoviride CBS 614.94 and endo-1,3(4)-beta-glucanase from Aspergillus tubingensis MUCL 39199 as silage additives for all animal species EFSA J. 2018 Apr 24;16(4):e05224.
8: Wang P, Wang P, Tian J, Yu X, Chang M, Chu X, Wu N. A new strategy to express the extracellular α-amylase from Pyrococcus furiosus in Bacillus amyloliquefaciens Sci Rep. 2016 Feb 26;6:22229.
9: Alikhajeh J, Khajeh K, Ranjbar B, Naderi-Manesh H, Lin YH, Liu E, Guan HH, Hsieh YC, Chuankhayan P, Huang YC, Jeyaraman J, Liu MY, Chen CJ. Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution: implications for thermal stability Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):121-9.
10: Ngalimat MS, Yahaya RSR, Baharudin MMA, Yaminudin SM, Karim M, Ahmad SA, Sabri S. A Review on the Biotechnological Applications of the Operational Group Bacillus amyloliquefaciens Microorganisms. 2021 Mar 17;9(3):614.

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