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Research Paper

Enzymatic characterization of D-lactate dehydrogenase and application in alanine aminotransferase activity assay kit

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Pages 6459-6471 | Received 05 Jul 2021, Accepted 21 Aug 2021, Published online: 13 Sep 2021

References

  • Kaplan MM. Alanine aminotransferase levels: what’s normal? Ann Intern Med. 2002;137:49–51.
  • Kim WR, Flamm SL, Di Bisceglie AM, et al. Serum activity of alanine aminotransferase (ALT) as an indicator of health and disease. Hepatology. 2008;47(4):1363–1370.
  • Rej R. Aspartate aminotransferase activity and isoenzyme proportions in human liver tissues. Clin Chem. 1978;24(11):1971–1979.
  • Tsai JF, Jeng JE, Ho MS, et al. Serum alanine aminotransferase level in relation to hepatitis B and C virus infections among blood donors. Liver. 1997;17(1):24–29.
  • Kochhar S, Chuard N, Hottinger H. Serum alanine aminotransferase level in relation to hepatitis B and C virus infections among blood donors. J Biol Chem. 1992;267(28):20298–20301.
  • Kochhar S, Hunziker PE, Leong-Morgenthaler P, et al. Primary structure, physicochemical properties, and chemical modification of NAD(+)-dependent D-lactate dehydrogenase. Evidence for the presence of Arg-235, His-303, Tyr-101, and Trp-19 at or near the active site. J Biol Chem. 1992;267(12):8499–8513.
  • Mu W, Yu S, Jiang B, et al. Characterization of D-lactate dehydrogenase from Pediococcus acidilactici that converts phenylpyruvic acid into phenyllactic acid. Biotechnol Lett. 2012;34(5):907–911.
  • Zheng ZJ, Ma CQ, Gao C, et al. Efficient conversion of phenylpyruvic acid to phenyllactic acid by using whole cells of bacillus coagulans SDM. PLoS One. 2011;6(4):e.19030.
  • Jia JH, Mu WM, Zhang T, et al. Bioconversion of phenylpyruvate to phenyllactate: gene cloning, expression, and enzymatic characterization of D- and L1-lactate dehydrogenases from Lactobacillus plantarum SK002. Appl Biochem Biotechnol. 2010;162(1):242–251.
  • Tokuda C, Ishikura Y, Shigematsu M, et al. Conversion of Lactobacillus pentosus d-Lactate Dehydrogenase to a d-Hydroxyisocaproate dehydrogenase through a single amino acid replacement. J Bacteriol. 2003;185(16):5023–5026.
  • Zhu YB, Hu FG, Zhu YY, et al. Enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from lactobacillus pentosus. Biotechnol Lett. 2015;37(6):1233–1241.
  • Hummel W, Schutte H, Kula MR. Large-scale production of D-lactate dehydrogenase for the stereospecific reduction of pyruvate and phenylpyruvate. Eur J Appl Microbiol Biotechnol. 1983;18(2):75–85.
  • Jun C, Sa YS, Gu S-A, et al. Discovery and characterization of a thermostable D-lactate dehydrogenase from Lactobacillus jensenii through genome mining. Process Biochem. 2013;48(1):109–117.
  • Liao YH, Brown MB, Quader A, et al. Protective mechanism of stabilizing excipients against dehydration in the freeze-drying of proteins. Pharm Res. 2002;19(12):1854–1861.
  • Bhatnagar BS, Bogner RH, Pikal MJ. Protein stability during freezing: separation of stresses and mechanisms of protein stabilization. Pharm Dev Technol. 2007;12(5):505–523.
  • Manning MC, Chou DK, Murphy BM, et al. Stability of protein pharmaceuticals: an update. Pharm Res. 2010;27:544–575.
  • Ohtake S, Kita Y, Arakawa T. Interactions of formulation excipients with proteins in solution and in the dried state. Adv Drug Deliv Rev. 2011;63:1053–1073.
  • Jeong SH. Analytical methods and formulation factors to enhance protein stability in solution. Arch Pharm Res. 2012;35(11):1871–1886.
  • Zhao G, Zhang G. Effect of protective agents, freezing temperature, rehydration media on viability of malolactic bacteria subjected to freeze-drying. J Appl Microbiol. 2005;99(2):333–338.
  • Zhan Y, Xu Q, Yang MM, et al. Screening of freeze-dried protective agents for the formulation of biocontrol strains, Bacillus cereus AR156, Burkholderia vietnamiensis B418 and Pantoea agglomerans 2Re40. Lett Appl Microbiol. 2012;54(1):10–17.
  • Iyengar ARS, Tripathy RK, Bajaj P, et al. Improving storage stability of recombinant organophosphorus hydrolase. Protein Expr Purif. 2015;111:28–35.
  • Zhou XH, Zhou J, Xin FX, et al. Heterologous expression of a novel D-lactate dehydrogenase from Lactobacillus sp ZX1 and its application for D phenyllactic acid production. Int J Biol Macromol. 2018;119:1171–1178.
  • Krieg RC, Dong Y, Schwamborn K, et al. Protein quantification and its tolerance for different interfering reagents using the BCA-method with regard to 2D SDS PAGE. J Biochem Biophys Methods. 2005;65(1):13–19.
  • Schumann C, Michlmayr H, Del Hierro AM, et al. Malolactic enzyme from Oenococcus oeni: heterologous expression in Escherichia coli and biochemical characterization. Bioengineered. 2013;4(3):147–152.
  • Li XF, Jiang B, Pan BL, et al. Purification and partial characterization of lactobacillus species SK007 Lactate Dehydrogenase (LDH) Catalyzing Phenylpyruvic Acid (PPA) Conversion into Phenyllactic Acid (PLA). J Agric Food Chem. 2008;56(7):2392–2399.
  • Kochhar S, Lamzin VS, Razeto A, et al. Roles of His205, His296, His303 and Asp259 in catalysis by NAD+-specific D-lactate dehydrogenase. Eur J Biochem. 2000;267(6):1633–1639.
  • Gu SA, Jun C, Joo JC, et al. Higher thermostability of L-lactate dehydrogenases is a key factor in decreasing the optical purity of D-lactic acid produced from Lactobacillus coryniformis. Enzyme Microb Technol. 2014;58-59:29–35.
  • Yang XL, Liu BZ, Sang Y, et al. Kinetic analysis of the lactate-dehydrogenase-coupled reaction process and measurement of alanine transaminase by an integration strategy. Anal Sci. 2010;26(11):1193–1198.
  • Gouda MD, Singh SA, Rao AGA, et al. Thermal inactivation of glucose oxidase - Mechanism and stabilization using additives. J Biol Chem. 2003;278(27):24324–24333.
  • Sawangwan T, Goedl C, Nidetzky B. Glucosylglycerol and glucosylglycerate as enzyme stabilizers. Biotechnol J. 2010;5(2):187–191.
  • Dabulis K, Klibanov AM. Dramatic enhancement of enzymatic activity in organic solvent by lyoprotectants. Biotechnol Bioeng. 1993;41(5):566–571.
  • Roy I, Gupta MN. Freeze-drying of proteins: some emerging concerns. Biotechnol Appl Biochem. 2004;39(2):165–177.
  • Xu H-M, Chen Y, Xu J, et al. Drug-induced liver injury in hospitalized patients with notably elevated alanine aminotransferase. World J Gastroenterol. 2012;18(41):5972–5978.
  • Galvin Z, McDonough A, Ryan J, et al. Blood alanine aminotransferase levels >1,000 IU/l – causes and outcomes. Clin Med (Lond). 2015;15(3):244–247.
  • Tamaki FK, Reece R. Directed evolution of enzymes. Emerg Top Life Sci. 2020;4(2):119–127.
  • Zhu LF, Xu XL, Wang LM, et al. NADP+-Preferring d-Lactate dehydrogenase from sporolactobacillus inulinus. Appl Environ Microbiol. 2015;81(18):6294–6301.
  • Yu S, Jiang H, Jiang B, et al. Characterization of D-Lactate Dehydrogenase producing D-3-Phenyllactic acid from pediococcus pentosaceus. Biosci Biotechnol Biochem. 2012;76(4):853–855.
  • Li C, Tao F, Xu P. Carbon Flux Trapping: highly Efficient Production of Polymer-Grade d-Lactic Acid with a Thermophilic d-Lactate Dehydrogenase. Chembiochem. 2016;17(16):1491–1494.
  • Fang R, Bogner RH, Nail SL, et al. Stability of freeze-dried protein formulations: contributions of ice nucleation temperature and residence time in the freeze-concentrate. J Pharm Sci. 2020;109(6):1896–1904.
  • Butreddy A, Janga KY, Ajjarapu S, et al. Instability of therapeutic proteins - An overview of stresses, stabilization mechanisms and analytical techniques involved in lyophilized proteins. Int J Biol Macromol. 2021;167:309–325.
  • Allison SD, Chang B, Randolph TW, et al. Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding. Arch Biochem Biophys. 1999;365(2):289–298.
  • Wang W, Ohtake S. Science and art of protein formulation development. Int J Pharm. 2019;568:118505.
  • Hansen LJJ, Daoussi R, Vervaet C, et al. Freeze-drying of live virus vaccines: a review. Vaccine. 2015;33(42):5507–5519.
  • Tonnis WF, Mensink MA, de Jager A, et al. Size and molecular flexibility of sugars determine the storage stability of freeze-dried proteins. Mol Pharm. 2015;12(3):684–694.
  • Forney-Stevens KM, Pelletier MJ, Shalaev EY, et al. Optimization of a Raman microscopy technique to efficiently detect amorphous–amorphous phase separation in freeze-dried protein formulations. J Pharm Sci. 2014;103(9):2749–2758.
  • Thakral S, Sonje J, Munjal B, et al. Stabilizers and their interaction with formulation components in frozen and freeze-dried protein formulations. Adv Drug Del Rev. 2021;173:1–19.
  • Bravo-Ferrada BM, Brizuela N, Gerbino E, et al. Effect of protective agents and previous acclimation on ethanol resistance of frozen and freeze-dried Lactobacillus plantarum strains. Cryobiology. 2015;71(3):522–528.