Extracellular amylolytic system of the yeast Lipomyces kononenkoae View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1979-09

AUTHORS

I. Spencer-Martins, N. van Uden

ABSTRACT

A strain of the yeast Lipomyces kononenkoae which converted starch into SCP with a high yield, produced three extracellular amylases which were purified from the culture fluid by Ficoll concentration, dialysis, isopropanol precipitation and DE-cellulose chromatography: an α-amylase, a glucoamylase and a debranching transferase. The latter transferred α-1,6-glucosyl units from panose to glucose forming maltose and appeared to have some debranching activity on amylopectin. The α-amylase had the following properties: MW 38000 daltons; no effect of added calcium ions on activity; optimum temperature and pH for activity around 40°C and pH 5.5; ΔH‡ and ΔS‡ of heat inactivation 24360 cal mol−1 and 29.2 cal deg−1 mol−1; range of pH stability pH 4–6.5; pI=7.1; final low molecular weight products of starch hydrolysis, maltose and glucose; Km (40°C, pH 5.5) for starch 2.7 gl−1, for maltotriose 109 gl−1; uncompetitive inhibition by maltose with Ki (40°C, pH 5.5) 29.5 gl−1. The glucoamylase had the following properties: MW 81500 daltons; optimum temperature and pH for activity around 50°C and pH 4.5: ΔH‡ and ΔS‡ of heat inactivation 20400 cal mol−1 and 17.7 cal deg−1 mol−1; range of pH stability pH 4–6.5; pI=6.1; Km (30°C, pH 4.5) for soluble starch 16.2 gl−1, for maltose 0.36 gl−1, for p-nitrophenyl-α-D-glucoside 0.35 gl−1; competitive inhibition by glucose with Ki (30°C, pH 4.5) 4.7 gl−1. More... »

PAGES

241-250

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00508096

DOI

http://dx.doi.org/10.1007/bf00508096

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1021519844


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