Mtwisha, LFarrant, JMBrandt, WHlongwane, CLindsey, GG2008-01-102008-01-102007-02Mtwisha, L et al. 2007. ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation. Functional Plant Biology, Vol. 34(2), pp 139-1491445-4408http://hdl.handle.net/10204/1827Copyright: 2007 Csiro PublishingASP53, a 53 kDa heat soluble protein, was identified as the most abundant protein in the mature seeds of Acacia erioloba E.Mey. Immunocytochemistry showed that ASP53 was present in the vacuoles and cell walls of the axes and cotyledons of mature seeds and disappeared coincident with loss of desiccation tolerance. The sequence of the ASP53 transcript was determined and found to be homologous to the double cupin domain-containing vicilin class of seed storage proteins. Mature seeds survived heating to 60°C and this may be facilitated by the presence of ASP53. Circular dichroism spectroscopy demonstrated that the protein displayed defined secondary structure, which was maintained even at high temperature. ASP53 was found to inhibit all three stages of protein thermal denaturation. ASP53 decreased the rate of loss of alcohol dehydrogenase activity at 55°C, decreased the rate of temperature-dependent loss of secondary structure of haemoglobin and completely inhibited the temperature-dependent aggregation of egg white protein.enCircular dichroism spectroscopyImmunocytochemistryProtection of protein conformationSeed storage proteinArticleMtwisha, L., Farrant, J., Brandt, W., Hlongwane, C., & Lindsey, G. (2007). ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation. http://hdl.handle.net/10204/1827Mtwisha, L, JM Farrant, W Brandt, C Hlongwane, and GG Lindsey "ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation." (2007) http://hdl.handle.net/10204/1827Mtwisha L, Farrant J, Brandt W, Hlongwane C, Lindsey G. ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation. 2007; http://hdl.handle.net/10204/1827.TY - Article AU - Mtwisha, L AU - Farrant, JM AU - Brandt, W AU - Hlongwane, C AU - Lindsey, GG AB - ASP53, a 53 kDa heat soluble protein, was identified as the most abundant protein in the mature seeds of Acacia erioloba E.Mey. Immunocytochemistry showed that ASP53 was present in the vacuoles and cell walls of the axes and cotyledons of mature seeds and disappeared coincident with loss of desiccation tolerance. The sequence of the ASP53 transcript was determined and found to be homologous to the double cupin domain-containing vicilin class of seed storage proteins. Mature seeds survived heating to 60°C and this may be facilitated by the presence of ASP53. Circular dichroism spectroscopy demonstrated that the protein displayed defined secondary structure, which was maintained even at high temperature. ASP53 was found to inhibit all three stages of protein thermal denaturation. ASP53 decreased the rate of loss of alcohol dehydrogenase activity at 55°C, decreased the rate of temperature-dependent loss of secondary structure of haemoglobin and completely inhibited the temperature-dependent aggregation of egg white protein. DA - 2007-02 DB - ResearchSpace DP - CSIR KW - Circular dichroism spectroscopy KW - Immunocytochemistry KW - Protection of protein conformation KW - Seed storage protein LK - https://researchspace.csir.co.za PY - 2007 SM - 1445-4408 T1 - ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation TI - ASP53, a thermostable protein from Acacia erioloba seeds that protects target proteins against thermal denaturation UR - http://hdl.handle.net/10204/1827 ER -