Tuning Thermostability and Catalytic Efficiency of Aflatoxin-Degrading Enzyme by Error-prone PCR

Jia, Ru; Tian, Shiwei; Yang, Zhongshan; Sadiq, Faizan Ahmed; Wang, Lan; Lu, Shaoyong; Zhang, Guohua; Li, Jianhui

doi:10.1007/s00253-023-12610-4

Cited by 3 publications

(1 citation statement)

References 63 publications

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“…Hydrogen bonds and hydrophobic interactions are crucial for protein stability, [11,33] which help maintain its conformational stability. [34] The total number of hydrogen bonds was increased in KdAKR M10 compared to that of KdAKR M6 (Table S4), contributing to its enhanced stability.…”

Section: Mechanism Elucidation For Stability Enhancementmentioning

confidence: 99%

Computer‐aided design to enhance the stability of aldo‐keto reductase KdAKR

Dai,

Tian,

Chen

et al. 2024

Biotechnology Journal

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The aldo‐keto reductase (AKR) KdAKR from Kluyvermyces dobzhanskii can reduce t‐butyl 6‐chloro‐(5S)‐hydroxy‐3‐oxohexanoate ((5S)‐CHOH) to t‐butyl 6‐chloro‐(3R,5S)‐dihydroxyhexanoate ((3R,5S)‐CDHH), which is the key chiral intermediate of rosuvastatin. Herein, a computer‐aided design that combined the use of PROSS platform and consensus design was employed to improve the stability of a previously constructed mutant KdAKRM6. Experimental verification revealed that S196C, T232A, V264I and V45L produced improved thermostability and activity. The “best” mutant KdAKRM10 (KdAKRM6‐S196C/T232A/V264I/V45L) was constructed by combining the four beneficial mutations, which displayed enhanced thermostability. Its T5015 and Tm values were increased by 10.2 and 10.0°C, respectively, and half‐life (t1/2) at 40°C was increased by 17.6 h. Additionally, KdAKRM10 demonstrated improved resistance to organic solvents compared to that of KdAKRM6. Structural analysis revealed that the increased number of hydrogen bonds and stabilized hydrophobic core contributed to the rigidity of KdAKRM10, thus improving its stability. The results validated the feasibility of the computer‐aided design strategy in improving the stability of AKRs.

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Section: Mechanism Elucidation For Stability Enhancementmentioning

confidence: 99%

Computer‐aided design to enhance the stability of aldo‐keto reductase KdAKR

Dai,

Tian,

Chen

et al. 2024

Biotechnology Journal

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The mitigative role of novel aflatoxin‐degrading enzymes in diverse broiler performance indicators and gut microbiota following the consumption of diets contaminated with aflatoxins

Jia,

Tian,

Yang

et al. 2024

J Sci Food Agric

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BACKGROUNDThis study aims to explore both the toxic effects of aflatoxins (AFs) and the protective effects of degrading enzymes (DE) on broilers exposed to AFs.RESULTSThe findings reveal that a diet contaminated with 69.15 μg kg−1 of aflatoxin B1 had significant adverse effects on broilers. Specifically, it led to a reduction in average daily gain, dressed yield percentage, half‐eviscerated yield with giblet yield percentage, eviscerated yield percentage, as well as serum superoxide dismutase (SOD), glutathione peroxidase activity and liver SOD activity (P < 0.05). Conversely, the diet increased the feed conversion ratio, liver index, serum glutamic oxaloacetic transaminase levels and malondialdehyde levels in both serum and liver (P < 0.05). Additionally, AFs disrupted the intestinal microflora significantly (P < 0.05), altering the relative abundance of Enterococcus, Lactobacillus and Escherichia in broiler jejunum. The addition of DE to AF‐contaminated feed mitigated these negative effects and reduced the residues of aflatoxin B1, aflatoxin B2 and aflatoxin M1 in the liver and duodenum (P < 0.05). We also observed that broilers fed the diet pelleted at 80 °C exhibited improved dressing percentage and water holding capacity compared to those on the 75 °C diet.CONCLUSIONIn summary, DE serves as an effective feed additive for mitigating AF contamination in poultry production. © 2024 Society of Chemical Industry.

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Engineering the terminal regions of Chondroitinase AC to improve the thermostability and activity

Huang,

Fan,

et al. 2024

Molecular Catalysis

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Tuning Thermostability and Catalytic Efficiency of Aflatoxin-Degrading Enzyme by Error-prone PCR

Cited by 3 publications

References 63 publications

Computer‐aided design to enhance the stability of aldo‐keto reductase KdAKR

Computer‐aided design to enhance the stability of aldo‐keto reductase KdAKR

The mitigative role of novel aflatoxin‐degrading enzymes in diverse broiler performance indicators and gut microbiota following the consumption of diets contaminated with aflatoxins

Engineering the terminal regions of Chondroitinase AC to improve the thermostability and activity

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