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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: Results show that some sorghums are rich sources of micronutrients (minerals and vitamins) and macronut nutrients (carbohydrates, proteins and fat) and that sorghum may be an alternative food for people who are allergic to gluten.
Abstract: Sorghum is a staple food grain in many semi-arid and tropic areas of the world, notably in Sub-Saharan Africa because of its good adaptation to hard environments and its good yield of production. Among important biochemical components for sorghum processing are levels of starch (amylose and amylopectin) and starch depolymerizing enzymes. Current research focus on identifying varieties meeting specific agricultural and food requirements from the great biodiversity of sorghums to insure food security. Results show that some sorghums are rich sources of micronutrients (minerals and vitamins) and macronutrients (carbohydrates, proteins and fat). Sorghum has a resistant starch, which makes it interesting for obese and diabetic people. In addition, sorghum may be an alternative food for people who are allergic to gluten. Malts of some sorghum varieties display α α α α-amylase and s-amylase activities comparable to those of barley, making them useful for various agro-industrial foods. The feature of sorghum as a food in developing as well as in developed countries is discussed. A particular emphasis is made on the impact of starch and starch degrading enzymes in the use of sorghum for some African foods, e.g. “to”, thin porridges for infants, granulated foods “couscous”, local beer “dolo”, as well agro-industrial foods such as lager beer and bread.

286 citations

Journal ArticleDOI
TL;DR: In this paper, a review of starch hydrolysis by specific amylases in model (in vitro ) and more broadly in in vivo systems is presented, where the authors discuss the optimal optimisation of starch metabolic enzymes and digestion in the light of modern knowledge.
Abstract: Digestion of starch is effected by hydrolysing enzymes in a complex process which depends on many factors; these include the botanical origin of starch, whether the starch is amorphous or crystalline, the source of enzymes, substrate and enzyme concentration, temperature and time, as well as the presence of other substances in the multicomponent matrix in which starch occurs naturally, e.g. cereal grains. Native starch is digested ( i.e. hydrolysed) slowly compared with processed (gelatinised) starch whose crystallinity has been lost and where the accessibility of substrate to enzymes is greater and not restricted by α-glucan associations such as double helices (especially in crystallites) or amylose-lipid complexes (in cereal starches). The restriction of starch digestion (primarily in the human digestive system) due to forms which are resistant to hydrolysis has led to the concept of dietary ‘resistant-starch’. Different forms of resistance can be identified which hinder hydrolysis. With regard to digestibility, whether in the human or animal digestive tract, it is important to understand the mechanisms of enzymatic hydrolysis, and the consequence of incomplete digestion i.e. the potential loss of glucose as a valuable source of energy. This review deals with starch hydrolysis by specific amylases in model ( in vitro ) and more broadly in in vivo systems. The optimisation of starch hydrolysis and digestion is discussed in the light of modern knowledge.

284 citations

Journal ArticleDOI
TL;DR: The production of protease by isolated aleurone layers of barley in response to gibberellic acid has been examined, giving some credence to the hypothesis that the effect of gibb Berellic Acid is to promote the simultaneous synthesis and secretion of a group of hydrolases.
Abstract: The production of protease by isolated aleurone layers of barley in response to gibberellic acid has been examined. The protease arises in the aleurone layer and is mostly released from the aleurone cells. The courses of release of amylase and protease from aleurone layers, the dose responses to gibberellic acid and the effects of inhibitors on the production of both enzymes are parallel. As is the case for amylase, protease is made de novo in response to the hormone. These data give some credence to the hypothesis that the effect of gibberellic acid is to promote the simultaneous synthesis and secretion of a group of hydrolases.

283 citations

Journal ArticleDOI
TL;DR: Investigation of factors that influence hydrolysis rates of starch in foods suggested that amylase inhibitor activity is destroyed by passage through the roller mill, since the starch in wheat germ and standard wholemeal flour was hydrolyzed at a rate identical to white flour.

283 citations

Journal Article
TL;DR: In vitro experiments showed that the amylase activity was inhibited in the presence of herbal extracts containing rosmarinic acid and purified RA, suggesting that other phenolic compounds or phenolic synergies may contribute to additional amyl enzyme inhibitory activity.
Abstract: Porcine pancreatic alpha-amylase (PPA) was allowed to react with herbal extracts containing rosmarinic acid (RA) and purified RA. The derivatized enzyme-phytochemical mixtures obtained were characterized for residual amylase activity. These in vitro experiments showed that the amylase activity was inhibited in the presence of these phytochemicals. The extent of amylase inhibition correlated with increased concentration of RA. RA-containing oregano extracts yielded higher than expected amylase inhibition than similar amount of purified RA, suggesting that other phenolic compounds or phenolic synergies may contribute to additional amylase inhibitory activity. The significance of food-grade, plant-based amylase inhibitors for modulation of diabetes mellitus and other oxidation-linked diseases is hypothesized and discussed.

280 citations


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