Soybean seed acid phosphatases: unusual optimum temperature and thermal stability studies

Biochemical and Biophysical Research Communications
Carmen Verissima FerreiraH Aoyama

Abstract

In contrast to other acid phosphatases, four cytoplasmic isoforms (AP1, AP2, AP3A, and AP3B) purified from mature soybean seeds presented high activities at temperatures above 80 degrees C, when p-nitrophenylphosphate (p-NPP) was utilized as substrate. However, with tyrosine phosphate and inorganic pyrophosphate as substrates, maximum activities were observed at temperature of 60 degrees C during 10 min reaction. In the absence of substrate, enzymes lost only 20% activity after 60 min at 60 degrees C; the isoforms AP3A and AP3B retained 30% of activity at 70 degrees C after 60 min and all the isoforms were inactivated at 80 degrees C, after 5 min. Thermal inactivation studies indicated that the soybean enzymes showed different temperature dependences in relation to most plant acid phosphatases. A best protective effect was observed when the isoforms were preincubated, at 70 degrees C, with phosphate (10 mM) and p-nitrophenol (10 mM) which indicates that the enzyme inactivation was prevented only in the presence of both reaction products.

Citations

Apr 19, 2015·Natural Product Research·Sanaullah KhanMushtaq Ahmed
Oct 7, 2006·Plant Physiology and Biochemistry : PPB·R SennaE Fialho
Apr 15, 2004·Phytochemistry·Alexandre Donizeti Martins CavagisHiroshi Aoyama
Aug 22, 2006·Archives of Insect Biochemistry and Physiology·D M P Oliveira, E A Machado
Apr 6, 2004·Plant Physiology and Biochemistry : PPB·Janaina Nicanuzia dos PrazeresHiroshi Aoyama

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