Porcine Pancreatic α-Amylase and its Isoforms: Purification and Kinetic Studies

Autor:	B. Anitha Gopal, G. Muralikrishna
Rok vydání:	2009
Předmět:	chemistry.chemical_classification Chromatography biology Size-exclusion chromatography Ion chromatography respiratory system Enzyme assay chemistry.chemical_compound Enzyme chemistry Biochemistry Maltotriose biology.protein Amylase Alpha-amylase Citric acid Food Science
Zdroj:	International Journal of Food Properties. 12:571-586
ISSN:	1532-2386 1094-2912
DOI:	10.1080/10942910801947755
Popis:	Porcine pancreatic α-amylase was separated on DEAE-cellulose into two isoforms, i.e., PPA-I and PPA-II and their molecular weight was found to be ∼ 55 kDa by gel filtration. The pH and temperature optima of PPA and its isoforms were 6.9 and 45°C. Chlorides of metal ions Ca2+, Ba2+, Co2+, and Mg2+ enhanced the enzyme activity, whereas Al3+ and Hg2+ completely inactivated the enzyme. Oxalic and citric acids inhibition of PPA and its isoforms is concentration dependant. EDTA was found to be the most effective inhibitor. PPA and its isoforms released maltotriose and maltotetraose from starches.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::db5f73aafde565abf076c4a326de5302 https://doi.org/10.1080/10942910801947755 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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