Stability of Murraya koenigii miraculin-like protein in different physicochemical conditions

Arakawa T, Timasheff SN (1985) Theory of protein solubility. Methods Enzymol 114:49–77

Azarkan M, Dibiani R, Goormaghtigh E, Raussens V, Baeyens-Volant D (2006) The papaya Kunitz-type trypsin inhibitor is a highly stable β-sheet glycoprotein. Biochim Biophys Acta 1764:1063–1072

Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein dye binding. Anal Biochem 72:248–254

Chaudhary NS, Shee C, Islam A, Ahmad F, Yernool D, Kumar P, Sharma AK (2008) Purification and characterization of a trypsin inhibitor from Putranjiva roxburghii seeds. Phytochemistry 69:2120–2126

Gahloth D, Selvakumar P, Shee C, Kumar P, Sharma AK (2010) Cloning, sequence analysis and crystal structure determination of a miraculin-like protein from Murraya koenigii. Arch Biochem Biophys 494:15–22

Kirk O, Borchert TV, Fuglsang CC (2002) Industrial enzyme applications. Curr Opin Biotechnol 13:345–351

Koshiyama I (1972) Purification and physico-chemical protperties of 11S globulin in soy bean seeds. Int J Pep Prot Res 4:167–176

Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685

Laskowski MJr, Kato I (1980) Protease inhibitors of proteinases. Annu Rev Biochem 49:593–626

Lehle K, Konert U, Stern A, Popp A, Jaenicke R (1996) Effect of disulfide bonds on the structure, function, and stabiltiy of the trypsin/tPA inhibitor from Erythrina caffra: site-directed mutagenesis, expression, and physiochemical characterization. Nat Biotechnol 14:476–480

Nyberg P, Ylipalosaari M, Sorsa T, Salo T (2006) Trypsins and their role in carcinoma growth. Exp Cell Res 312:1219–1228

Onesti S, Brick P, Blow DM (1991) Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds. J Mol Biol 217:153–156

Ries-Kautt M, Ducruix A (1997) Inferences drawn from physicochemical studies of crystallogenesis and precrystalline state. Methods Enzymol 276:23–59

Roy I, Gupta MN (2003) pH-responsive polymer-assisted refolding of urea- and organic solvent-denatured α-chymotrypsin. Protein Eng 16:1153–1157

Roychaudhuri R, Sarath G, Zeece M, Markwell J (2003) Reversible denaturation of the soybean Kunitz trypsin inhibitor. Arch Biochem Biophys 412:20–26

Roychaudhuri R, Sarath G, Zeece M, Markwell J (2004) Stability of the allergenic soybean Kunitz trypsin inhibitor. Biochim Biophys Acta 1699:207–212

Royer CA (1995) Approaches to teaching fluorescence spectroscopy. Biophys J 68:1191–1196

Schaefer M, Sommer M, Karplus M (1997) pH-dependence of protein stability: absolute electrostatic free energy differences between conformations. J Phys Chem B 101:1663–1683

Shan L, Li C, Chen F, Zhao S, Xia G (2008) A Bowman-Birk type protease inhibitor is involved in the tolerance to salt stress in wheat. Plan Cell Environ 31:1128–1137

Shee C, Sharma AK (2007) Purification and characterization of a trypsin inhibitor from seeds of Murraya koenigii. J Enzym Inhib Med Chem 22:115–120

Shee C, Sharma AK (2008) Storage and affinity properties of Murraya koenigii trypsin inhibitor. Food Chem 107(1):312–319

Shee C, Islam A, Ahmad F, Sharma AK (2007a) Structure-function studies of Murraya koenigii trypsin inhibitor revealed a stable core beta sheet structure surrounded by alpha-helices with a possible role for alpha-helix in inhibitory function. Int J Biol Macromol 41(4):410–414

Shee C, Singh TP, Kumar P, Sharma AK (2007b) Crystallization and preliminary X-ray diffraction studies of Murraya koenigii trypsin inhibitor. Acta Crystallogr Sect F 63:318–319

Shen LJ (1976) Solubility profile, intrinsic viscosity, and optical rotation studies of acid precipitated soy protein and commercial soy isolate. J Agric Food Chem 24:784–789

Shibata H, Hara S, Ikenaka T, Abe J (1986) Purification and characterization of proteinase inhibitors from winged bean (Psophocarpus tetragonolobus (L.) (DC.) seeds. J Biochem 99:1147–1155

Sweet RM, Wright HT, Janin J, Chothia CH, Blow DM (1974) Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-Å resolution. Biochemistry 13:4212–4228

Tanford C (1968) Protein denaturation. Adv Protein Chem 23:122–282

Theerasilp S, Kurihara Y (1988) Complete purification and characterization of the taste-modifying protein, miraculin, from miracle fruit. J Biol Chem 263(23):11536–11539

Tsukuda S, Gomi K, Yamamoto H, Akimitsu K (2006) Characterization of cDNAs encoding two distinct miraculin-like proteins and stress-related modulation of the corresponding mRNAs in Citrus jambhiri Lush. Plant Mol Biol 60:125–136

Ullmann GM, Knapp EW (1999) Electrostatic models for computing protonation and redox equilibria in proteins. Eur Biophys J 28:533–551

Wolf WJ, Tamura T (1969) Heat denaturation of soy bean 11S protein. Cereal Chem 46:331–344

Woradulayapinij W, Soonthornchareonnon N, Wiwat C (2005) In vitro HIV type 1 reverse transcriptase inhibitory activities of Thai medicinal plants and Canna indica L. rhizomes. J Ethnopharmacol 101(1–3):84–89

Yang AS, Honig B (1993) On the pH dependence of protein stability. J Mol Biol 231:459–474