US 12,312,612 B2
Acid phosphatase mutants and methods of using the same
Liming Liu, Wuxi (CN); Xin Xu, Wuxi (CN); Wei Song, Wuxi (CN); Xiulai Chen, Wuxi (CN); Jia Liu, Wuxi (CN); Cong Gao, Wuxi (CN); Jing Wu, Wuxi (CN); and Liang Guo, Wuxi (CN)
Assigned to Jiangnan University, Wuxi (CN)
Filed by Jiangnan University, Wuxi (CN)
Filed on Mar. 15, 2022, as Appl. No. 17/694,779.
Application 17/694,779 is a continuation of application No. PCT/CN2021/096674, filed on May 28, 2021.
Claims priority of application No. 202110388771.2 (CN), filed on Apr. 12, 2021.
Prior Publication US 2022/0204953 A1, Jun. 30, 2022
Int. Cl. C12N 9/16 (2006.01); C12N 15/70 (2006.01); C12P 17/04 (2006.01)
CPC C12N 9/16 (2013.01) [C12N 15/70 (2013.01); C12P 17/04 (2013.01); C12Y 301/03002 (2013.01)] 1 Claim
 
1. An acid phosphatase mutant, wherein the acid phosphatase mutant is from Pseudomonas aeruginosa (P. aeruginosa),
wherein the acid phosphatase mutant comprises the amino acid sequence of SEQ ID NO:1 with mutations at any one or more of sites 57, 58, 94, or 135 of SEQ ID NO: 1,
wherein the acid phosphatase mutant possesses a catalytic efficiency that is greater than the catalytic efficiency of a corresponding wild type acid phosphatase from P. aeruginosa, and
wherein the mutations are in any one or more of (a)-(f):
(a) the site 58 is mutated into phenylalanine;
(b) the site 94 is mutated into phenylalanine;
(c) the site 135 is mutated into arginine;
(d) the site 94 is mutated into phenylalanine, and the site 135 is mutated into arginine;
(e) the site 58 is mutated into proline, and the site 135 is mutated into arginine; or
(f) the site 57 is mutated into histidine, the site 58 is mutated into proline, and the site 135 is mutated into arginine.