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Amylase

About: Amylase is a research topic. Over the lifetime, 14164 publications have been published within this topic receiving 296069 citations.


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Journal ArticleDOI
TL;DR: Two sets of alpha-amylase seem to exist in lentil cotyledons based on their heat lability or heat stability, and several independent criteria show that the amylolytic activity is due mainly to an amylase of the alpha type.
Abstract: Starch, total amylolytic and phosphorylase activities were determined in lentil cotyledons during the first days of germination. Several independent criteria show that the amylolytic activity is due mainly to an amylase of the alpha type. Starch is degraded slowly in the first days; during this time, alpha- and beta-amylase activity are very low, while phosphorylase increases and reach a peak on the 3rd day. On the 4th day, there is a more rapid depletion of starch which coincides with an increase in alpha-amylase activity. By polyacrylamide gel electrophoresis of the crude starch-degrading enzyme, five bands were obtained: one phosphorylase, three alpha-amylases, and one beta-amylase. Based on their heat lability or heat stability, two sets of alpha-amylase seem to exist in lentil cotyledons.

75 citations

Journal ArticleDOI
TL;DR: The amylase from B .

75 citations

Journal ArticleDOI
TL;DR: This work studied amylase, lipase, polygalacturonase and protease production by fifty-six isolates of Mucor belonging to 11 different taxa, selected from herbivores dung using solid media and showed that the majority of the isolates presented several enzymatic activities.

75 citations

01 Jan 2005
TL;DR: The enzyme tests indicate that most endophytes are degraders of the simpler sugars and cellulose available in recently dead leaves and possibly wood.
Abstract: Twenty-one endophytic isolates from Brucea javanica were tested for their ability to produce extracellular cellulase and extracellular and intracellular amylase, ligninase, pectinase and xylanase. The same fungi were tested for their ability to cause weight loss in wood blocks. All fungi produced amylase and cellulase, while only one sterile mycelium produced ligninase and no isolates produced pectinase. The enzyme tests indicate that most endophytes are degraders of the simpler sugars and cellulose available in recently dead leaves and possibly wood. Only one slow growing species of sterile mycelium however, appeared to be capable of degrading lignin that would be available in dead wood. No fungi appeared to be latent pathogens. A discussion of enzyme production in relation to possible roles of endophytes is provided.

75 citations

Journal ArticleDOI
TL;DR: In this article, the influence of α-amylase on bread crumbs and on wheat starch gels was investigated taking into account different levels of structural hierarchy, and the effect of α amylase was shown to enhance the initial firmness of bread and reduce the firming rate of wheat gels on aging.
Abstract: The influence of an antistaling α-amylase on bread crumb and on wheat starch gels was investigated taking into account different levels of structural hierarchy. Bread was prepared by a conventional baking procedure. Starch gels were produced by heating a concentrated starch dispersion in closed molds. Bread and starch gels were characterized by compression tests, light microscopy (LM), differential scanning calorimetry, and X-ray measurements. The α-amylase enhanced the initial firmness of starch gels and reduced the firming rate of bread and starch gels on aging. LM revealed that amylose and amylopectin phase-separated within the starch granules and that freshly baked control bread and starch gels showed weak birefringence which became more intense during aging. Amylase-containing bread and starch gels exhibited strong birefringence in the amylose rich region of the granules directly after baking which did not significantly increase during aging. The enzyme hindered the retrogradation of amylope...

75 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20241
2023460
2022976
2021308
2020347
2019328