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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1986-3-5
pubmed:abstractText
Three forms of glucoamylase [EC 3.2.1.3] of a Rhizopus sp., Gluc1 (M.W. 74,000), Gluc2 (M.W. 58,600), and Gluc3 (M.W. 61,400), which have similar pH optima and specific activities towards soluble starch were studied as to their behavior towards raw starch. The pH optima for raw starch digestion were different, that is, 4.5 for Gluc1 and 5.0 for both Gluc2 and Gluc3. All the enzymes digested raw starch almost completely but at quite different rates; Gluc2 and Gluc3, which lack the N-terminal portions of Gluc1, were 22 and 25 times less effective, respectively, for raw starch digestion than Gluc1. Of the three enzymes, only Gluc1 tightly bound to raw starch. Binding of Gluc1 to raw starch occurred pH-dependently with a broad pH optimum of 4.5-5.5, but temperature and ionic strength affected it only slightly and little, respectively. The binding constant of Gluc1 for raw starch at pH 5.0 and 4 degrees C was estimated to be 1.2 X 10(5) M-1. Fragment H (M.W. 16,700), presumably released from the N-terminal part of Gluc1, not only bound to raw starch itself but also inhibited the binding of Gluc1 to raw starch. pap-Gluc (M.W. 57,000) and chymo-Gluc (M.W. 64,000), which are papain- and chymotrypsin-modified Gluc1, respectively, and lack the N-terminal portions of Gluc1, resembled Gluc2 and Gluc3 in raw starch binding as well as digestion. All these results indicate that Gluc1 has a raw starch-binding site, different from the active center, in the N-terminal region. Various substrates and analogs inhibited the binding of Gluc1 to raw starch, presumably due to steric hindrance.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
98
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
663-71
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Different behavior towards raw starch of three forms of glucoamylase from a Rhizopus sp.
pubmed:publicationType
Journal Article