1968
DOI: 10.1002/star.19680200502
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Studies on Starch‐Degrading Enzymes. Part VIII A Comparison of α‐Amylases from Different Sources: Their Properties and Action Patterns

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Cited by 41 publications
(12 citation statements)
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“…Purified enzyme preparations have limited stability at mashing temperatures unless protected by neutral protein or by the presence of an excess of substrate.8-21 How ever, the protection normally provided by the mash constituents can be replaced by having an excess of calcium ions in the 10 Enzyme stability was therefore maintained in the starch granule digests by adding sufficient calcium chloride (10-mM) to stabilize the a-amylase over a range of pH values at 65°C (Table III).…”
Section: Resultsmentioning
confidence: 99%
“…Purified enzyme preparations have limited stability at mashing temperatures unless protected by neutral protein or by the presence of an excess of substrate.8-21 How ever, the protection normally provided by the mash constituents can be replaced by having an excess of calcium ions in the 10 Enzyme stability was therefore maintained in the starch granule digests by adding sufficient calcium chloride (10-mM) to stabilize the a-amylase over a range of pH values at 65°C (Table III).…”
Section: Resultsmentioning
confidence: 99%
“…2). This histidine residue is required for activity of the enzymes from plants, animals, bacteria and from fungi (Greenwood and Milne, 1968;Kita et al, 1982;Dua and Kochhar, 1985). It is interesting to note that two residues equivalent to Pro 129 and Pro 137 are present in AMY2 isoform in barley and which are substituted by lysine and leucine amino acid in case of AMY1.…”
Section: Substratementioning
confidence: 98%
“…Starch can be separated into amylose, a linear macromolecule and amylopcctin, a branched glycogen-like polymer in proportions depending on the plant from which the starch originates [Deatherage et al, 1955], The ultimate products from com plete «-amylolysis of both components are glucose and maltose [for review : Banks and Greenwood, 1975], the a-amylase of saliva producing predominantly maltose and mal totriose [Greenwood and Milne, 1968;Mormann-Buchmann, 1979]. Despite the fact that a-amylase is present in consider able amounts in human parotid saliva [Ja cobsen et al, 1972], no attempt has been made to quantify the mode and rate of amylolytic hydrolysis of dietary starch in vivo.…”
mentioning
confidence: 99%