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|Title:||Enzyme-stabilizing activity of seed trypsin inhibitors during desiccation||Authors:||Lam, J.-M.
Kunitz trypsin inhibitor
|Issue Date:||29-Mar-1999||Citation:||Lam, J.-M., Pwee, K.-H., Sun, W.Q., Chua, Y.-L., Wang, X.-J. (1999-03-29). Enzyme-stabilizing activity of seed trypsin inhibitors during desiccation. Plant Science 142 (2) : 209-218. ScholarBank@NUS Repository. https://doi.org/10.1016/S0168-9452(99)00007-2||Abstract:||Seeds contain protective proteins which are able to preserve glucose-6- phosphate dehydrogenase (EC 220.127.116.11) activity upon co-dehydration of the enzyme with heat-stable seed protein extracts. Adenanthera pavonina L. (saga) seed extracts, in particular, have high levels of enzyme-preserving activity which not only alleviate the detrimental effects of desiccation in the presence of Tris-HCl and NaCl, but also stabilize enzyme activity in solution. Purification of Adenanthera seed extracts by reversed-phase and weak anion-exchange perfusion chromatography, followed by N-terminal protein sequencing have identified Kunitz-type trypsin inhibitors as the major proteins in one set of enzyme-preserving fractions. A quantitative comparison using various concentrations of purified proteins has demonstrated that soybean Kunitz trypsin inhibitor is as effective (on a mass basis) as bovine serum albumin in preserving enzyme activity, and may be an important protein permitting enzyme dehydration in a seed undergoing desiccation.||Source Title:||Plant Science||URI:||http://scholarbank.nus.edu.sg/handle/10635/100595||ISSN:||01689452||DOI:||10.1016/S0168-9452(99)00007-2|
|Appears in Collections:||Staff Publications|
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