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Bacillus Licheniformis α-amylase: Structural Feature in a Biomimetic Solution and Structural Changes in Extrinsic Conditions

Bacillus Licheniformis α-amylase: Structural Feature in a Biomimetic Solution and Structural Changes in Extrinsic Conditions

Jongchan Lee, Li Xiang, Sumiya Byambabaatar, Heesoo Kim, Kyeong Sik Jin, Moonhor Ree

Int J Biol Macromol. 2019 Apr 15;127:286-296.

PMID: 30654032

Abstract:

Bacillus licheniformis α-amylase (BLA) in a biomimetic buffer and extrinsic solutions (various pH values, temperatures, and metal ions) has been investigated for the first time in the view of three-dimensional (3D) structure by synchrotron X-ray and dynamic light scattering analyses. BLA in buffer is determined to have a structure resembling its crystallographic structure; but the 3D structure is slightly larger than the crystal structure. Such a structure is maintained with little variations in extrinsic solutions of pH 4.0-9.7, temperature 4-55 °C, and metal ions such as Ba2+, Mg2+, and Li+. These results collectively inform that BLA tends to favorably form a stable monomeric structure, which could provide structural clues to its enzymatic activities in moderate levels. Interestingly, BLA is found to reveal highly expanded structures at 65-75 °C and in Co2+ solution, which could correlate to the significantly pronounced enzymatic activities. However, BLA shows somewhat shrunken structures at pH 3.0 and in Hg2+ solution, supporting for the suppressed activities under these conditions.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9000855-C	α-Amylase from Bacillus licheniformis		9000-85-5	Price

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