Characterization of a Novel Mannose Isomerase from Stenotrophomonas rhizophila and Identification of Its Possible Catalytic Residues

Wu, Yue; Huang, Zhaolin; Zhang, Wenli; Guang, Cuie; Chen, Qiuming; Mu, Wanmeng

doi:10.1007/s12033-021-00437-1

Cited by 6 publications

(4 citation statements)

References 28 publications

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“…The substrate specificity of Xp MIaseA toward d -mannose (355.1 U mg –1 ) is lower than that of Strh -MIase from Stenotrophomonas rhizophila (437.5 U mg –1 ), but it is much higher than those of most other d -mannose isomerases, such as those from A. radiobacter (231.0 U mg –1 ), Pseudomonas geniculata (295.3 U mg –1 ), and T.…”

Section: Resultsmentioning

confidence: 87%

“…Moreover, after the reaction reached equilibrium, 68.1% of M2 was converted to MF, as indicated by the 2.1:1 ratio of MF to M2 in the reaction system. This finding is reasonable because the conversion ratios of d -mannose to d -fructose achieved using most mannose isomerases range from 60% to 75%. , Therefore, the one-pot three-enzyme system, using the inexpensive substrate mannan, served as an effective bioconversion strategy for MF production.…”

Section: Resultsmentioning

confidence: 99%

“…Therefore, most Dmannose isomerases do not isomerize disaccharides. 5,30 In XpMIaseA, Phe247 was located in the α7-α8 loop, whereas no matching Trp was found in the α11-α12 loop (Figure 4D). The hydrophobic interaction between α11-α12 loop and D- mannose disappears, and the hydrophobic interaction of α7-α8 loop with α11-α12 loop and D-mannose is weakened.…”

Section: Putative Model Ofmentioning

confidence: 99%

“…This finding is reasonable because the conversion ratios of D-mannose to D-fructose achieved using most mannose isomerases range from 60% to 75%. 5,30 Therefore, the one-pot three-enzyme system, using the inexpensive substrate mannan, served as an effective bioconversion strategy for MF production.…”

Section: One-pot Production Of Mfmentioning

confidence: 99%

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One-Pot Three-Enzyme System for Production of a Novel Prebiotic Mannosyl-β-(1 → 4)-Fructose Using a d-Mannose Isomerase from Xanthomonas phaseoli

Xiaohan

Yan

et al. 2022

J. Agric. Food Chem.

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The present supply of prebiotics is entirely inadequate to meet their demand. To produce novel prebiotics, a d-mannose isomerase (XpMIaseA) from Xanthomonas phaseoli was first produced in Komagataella phaffii (Pichia pastoris). XpMIaseA shared the highest amino acid sequence identity (58.0%) with the enzyme from Marinomonas mediterranea. Efficient secretory production of XpMIaseA (282.0 U mL–1) was achieved using high cell density fermentation. The optimal conditions of XpMIaseA were pH 7.5 and 55 °C. It showed a broad substrate specificity, which isomerized d-mannose, d-talose, mannobiose, epilactose, and mannotriose. XpMIaseA was employed to construct a one-pot three-enzyme system for the production of mannosyl-β-(1 → 4)-fructose (MF) using mannan (5%, w/v) as the substrate. The equilibrium yield of MF was 58.2%. In in vitro fermentations, MF significantly stimulated (≤3.2-fold) the growth of 12 among 15 tested Bifidobacterium and Lactobacillus strains compared with fructo-oligosaccharides. Thus, the novel d-mannose isomerase provides a one-pot bioconversion strategy for efficiently producing novel prebiotics.

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