[1] Lucia, F. and Tomas, G.V. (2010) Native and biotechnologically engineered plant proteases with industrial applications. Food and Bioprocess Technology, 4, 1066- 1088.
[2] Dubey, V.K. and Jagannadham, M.V. (2003) Procerain, a stable cysteine protease from the latex of Calotropis prcera. Phytochemisty, 62, 1057-1071. Hdoi:10.1016/S0031-9422(02)00676-3
[3] Kelly, G.S. (1996) Bromelain: A literature review and discussion of its therapeutic applications. Alternative Medicine Review, 1, 243-257.
[4] Maurer, H.R. (2001) Bromelain: Biochemistry, pharmacology and medical uses. Cellular and Molecular Life Sciences, 58, 1234-1245. Hdoi:10.1007/PL00000936H
[5] Tochi, B.N., Wang, Z., Xu, S.Y. and Zhang, W. (2009) Effect of stem bromelain on the browning of apple juice, American Journal of Food Technology, 10, 1-8.
[6] Aehle, W. (2007) Enzymes in Industry: Production and Applications. Wiley-VCH/Verlag GmbH and Co., Weinheim, 6.
[7] Walsh, G. (2002) Protein Biochemistry and Biotechnology. John Wiley and Sons, New York, 312.
[8] Koh, J., Kang, S.M., Kim, S.J., Cha, M.K. and Kwon, Y.J. (2006) Effect of pineapple protease on the characteristics of protein fibers. Fibers and Polymers, 7, 180-185. Hdoi:10.1007/BF02908264
[9] Ketnawa, S., Rawdkuen, S. and Chaiwut, P. (2010) Two phase partitioning and collagen hydrolysis of bromelain from pineapple peel Nang Lae cultivar. Biochemical Engineering Journal, 52, 205-211. Hdoi:10.1016/j.bej.2010.08.012
[10] Yuan, G., Wahlqvist, M.L., He, G., Yang, M. and Li, D. (2006) Natural products and anti-inflammatory activity. Asia Pacific Journal of Clinical Nutrition, 15,143-152.
[11] Illanes A. (2008) Enzyme Biocatalysis. Springer Science and Business Media V.B., Brazil, 69. Hdoi:10.1007/978-1-4020-8361-7
[12] Amid, A., Ismail, N., Yusof, F. and Salleh, H.M. (2011) Expression, purification and characterization of a recombinant stem bromelain from Ananas comosus. Process Biochemistry, 46, 2232-2239. Hdoi:10.1016/j.procbio.2011.08.018
[13] Bala, M., Amid, A., Mel, M., Jami, S. and Salleh, H.M. (2011) Recovery of recombinant bromelain from Escherichia coli BL21-AI. African Journal of Biotechnology, 10, 8829-18832. Hdoi:10.5897/AJB11.2761
[14] Muntari, B., Salleh, H.M., Amid, A., Mel, M. and Jami, M.S. (2012) Recombinant bromelain production in Escherichia coli: Process optimization in shake flask culture by Response Surface Methodology. AMB Express, 2, 1-9. Hdoi:10.1186/2191-0855-2-12
[15] Ismail, N. and Amid, A. (2012). Differential scanning calorimetry as tool in observing thermal and storage stability of recombinant bromelain. Food Research International, 19, 727-731.
[16] Laemmli, U. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 237, 680-685. Hdoi:10.1038/227680a0
[17] Bradford, M.M. (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Analytical Biochemistry, 72, 248-254. Hdoi:10.1016/0003-2697(76)90527-3
[18] Silverstein, R.M. (1974) The assay of the bromelains using N-CBZ-L-lysine-p-nitrophenylester and N-CBZ-L-gly-cine-p-nitrophenyl ester as substrates. Analytical Biochemistry, 62, 478-484. Hdoi:10.1016/0003-2697(74)90180-8
[19] Filippova, I., Lyso-gorskaya, E.N., Oksenoit, E.S., Ruden- skaya, G.N., Stepanov, V.M. (1984) L-Pyroglutamyl-l-phenylala-nyl-l-leucine-p-nitroanilide—A chromogenic substrate for thiol proteinase assay. Analytical Biochemistry, 143, 293-297. Hdoi:10.1016/0003-2697(84)90665-1
[20] Rowan, A.D. and Buttle, D.J. (1994) Pineapple cysteine endopeptidases. Methods in Enzymology, 244, 555-568. Hdoi:10.1016/0076-6879(94)44040-9
[21] Valle, D.M., Bruno, M., Laura, L.M.I., Caffini, N.O., Cantera, A.M.B. (2008) Granulosain I, a Cysteine Protease isolated from ripe fruits of solanum granuloso-leprosum (Solanaceae). The Protein Journal, 27, 267-275. Hdoi:10.1007/s10930-008-9133-4
[22] Benucci, I., Liburdi, K., Garzillo, A.M.V. and Esti, M. (2011) Bromelain from pineapple stem in alcoholic-acidic buffers for wine application. Food Chemistry, 124, 1349- 1353. Hdoi:10.1016/j.foodchem.2010.07.087
[23] Morcelle, S.R., Trejo, A.S., Canals, F., Avilés, F.X., Priolo, N.S. (2004) Funastrain c II: A cysteine endopeptidase purified from the latex of Funastrum clause. The Protein Journal, 23, 205-215. Hdoi:10.1023/B:JOPC.0000026416.90134.7b
[24] Napper, A.D., Bennett, P., Borowski, M., Holdridge, M.B., Leonard, M.J.C., Rogers, E.E., Duan, Y., Laursen, R.A., Reinhold, B.S. and Hames, S.L. (1994) Purification and characterization of multiple forms of the pineapplestem-derived cysteine proteinases ananain and comosain. Biochemical Journal, 301, 727-735.
[25] Liggieri, M., Arribe, C., Trejo, S.A., Canals, F., Avile, F.X. and Priolo, N.S. (2004) Purification and biochemical characterization of Asclepain c I from the latex of Asclepias curassavica L. constanza. The Protein Journal, 23, 403-411. Hdoi:10.1023/B:JOPC.0000039554.18157.69
[26] M Bruno, M.A., Trejo, S.A., Aviles, X.F., Caffini, N.O. and Lopez, L.M. (2006). Isolation and characterization of Hieronymain II, another peptidase isolated from fruits of Bromelia hieronymi Mez (Bromeliaceae). The Protein Journal, 25, 224-223. Hdoi:10.1007/s10930-006-9005-8
[27] Perez, A., Carvajal, C., Trejo, S., Torres, M.J., Martin, M.I., Lorenzo, J.C., Natalucci, C.L. and Hernandez, M. (2010) Penduliflorain I: A cysteine protease isolated from Hohenbergia penduliflora (A.Rich.) Mez (Bromeliaceae). The Protein Journal, 29, 225-233. Hdoi:10.1007/s10930-010-9243-7
[28] Novillo, C., Casta, P. and Ortego, F. (1997) Inhibition of digestive trypsin-like proteases from larvae of several lepidopteran species by the diagnostic cysteine protease inhibitor E-64. Insect Biochemistry and Molecular Biology, 27, 247-254. Hdoi:10.1016/S0965-1748(96)00092-6
[29] Sreedharan, S.K., Patel, H., Smith, S., Gharbia, S.E., Shah, H.N. and Brocklehurst, K. (1993) Additional evidence for the cysteine proteinase nature of gingivain the extracellular proteinase of Porphyromonas gingivalis. Biochemical Society Transactions, 21, 218S-218S.
[30] Sreedharan, S.K., Verma, C., Caves, L.S.D., Brocklehurst, S.M., Gharbias, S.E., Shah, H.N. and Brocklehurst, K. (1996) Demonstration that 1-trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane (E-64) is one of the most effective low Mr inhibitors of trypsin-catalysed hydrolysis, Characterization by kinetic analysis and by energy minimization and molecular dynamics simulation of the E-64-13-trypsin complex. Biochemical Journal, 316, 777- 786.