Hotspot-based mutation engineering of MAase from Lactobacillus rhamnosus YXY412 for the improvement of hydrolytic activity-Reference-Cited by-同舟云学术

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Hotspot-based mutation engineering of MAase from Lactobacillus rhamnosus YXY412 for the improvement of hydrolytic activity

Published:2024-04-26 Issue:3 Volume:4 Page:941-952
ISSN:2662-7655
Container-title:Systems Microbiology and Biomanufacturing
language:en
Short-container-title:Syst Microbiol and Biomanuf

Author:

Su Xiaoya,Zhang Dong,Huang Jing,Lei Yuqing,Huang Weining,Wu Minchen

Funder

Postdoctoral Science Foundation of China

National Key Special Project for the 13th National 5-Year Plan Program of China

Publisher

Springer Science and Business Media LLC

Link

https://link.springer.com/content/pdf/10.1007/s43393-024-00261-z.pdf

Reference36 articles.

1. Bertoldo C, Antranikian G. Starch-hydrolyzing enzymes from thermophilic archaea and bacteria. Curr Opin Chem Biol. 2002;6:151–60. https://doi.org/10.1016/s1367-5931(02)00311-3.

2. Park KH, Kim TJ, Cheong TK, Kim JW, Oh BH, Svensson B. Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family. Biochim Biophys Acta. 2000;1478:165–85. https://doi.org/10.1016/s0167-4838(00)00041-8.

3. Stam MR, Danchin EG, Rancurel C, Coutinho PM, Henrissat B. Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of alpha-amylase-related proteins. Protein Eng Des Sel. 2006;19:555–62. https://doi.org/10.1093/protein/gzl044.

4. Saburi W, Morimoto N, Mukai A, Kim DH, Takehana T, Koike S, Matsui H, Mori H. A thermophilic alkalophilic alpha-amylase from Bacillus sp AAH-31 shows a novel domain organization among glycoside hydrolase family 13 enzymes. Biosci Biotechnol Biochem. 2013;77:1867–73. https://doi.org/10.1271/bbb.130284.

5. Shim JH, Park JT, Hong JS, Kim KW, Kim MJ, Auh JH, Kim YW, Park CS, Boos W, Kim JW, Park KH. Role of maltogenic amylase and pullulanase in maltodextrin and glycogen metabolism of Bacillus subtilis 168. J Bacteriol. 2009;191:4835–44. https://doi.org/10.1128/JB.00176-09.

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