期刊
PLANT PHYSIOLOGY AND BIOCHEMISTRY
卷 69, 期 -, 页码 49-53出版社
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.plaphy.2013.04.017
关键词
Plant seed; Characterization; Substrate specificity; Degradation
资金
- National Grants of China [2010CB732202]
An acidic alpha-galactosidase (EC 3.2.1.22) designated as Phaseolus coccineus seeds galactosidase (PCG) was purified from P. coccineus seeds using ion-exchange chromatography on DEAE- and CM-cellulose, Q- and SP-Sepharose and gel filtration on Superdex 75. The molecular weight of PCG was 43 kDa as judged by SDS PAGE and gel filtration. Two inner peptides of PCG were sequenced by MALDI-TOF-MS. The optimum pH and temperature was 3.0 and 70 degrees C, respectively but was stable up to 60 degrees C for 30 min. The enzyme activity was inhibited by NBS signifying the pivotal role played by tryptophan in the catalytic activity of the enzyme. The K-m for hydrolysis of pNPGal was 0.0025 mM. Besides hydrolyzing pNPGal, agalactosidases also hydrolyzed natural substrates such as melibiose, raffinose and stachyose. Hence it can be exploited commercially for improving the nutritional value of soymilk. Thus the PCG has great potential in the feed industries for removal of non-digestible oligosaccharide from legumes. (C) 2013 Elsevier Masson SAS. All rights reserved.
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