Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Sucrose isomerases as food and nutritional supplements

A technology of sucrose isomerase and nutritional supplements, applied in the field of sucrose isomerase, can solve the problems of being expensive and affecting the taste of the final product

Pending Publication Date: 2021-03-26
DSM IP ASSETS BV
View PDF18 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The lower sweetness must be compensated by, for example, adding additional artificial sweeteners, which may affect the taste of the final product
Also, isomaltulose is relatively expensive compared to sucrose, so it may not be added to food or beverage products for economical reasons

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Sucrose isomerases as food and nutritional supplements
  • Sucrose isomerases as food and nutritional supplements
  • Sucrose isomerases as food and nutritional supplements

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0064] Sucrose Isomerase

[0065] Six proteins annotated as sucrose isomerases were selected from the Uniprot database. The sequences were derived from P. rubrum (Uniprot: DOVX20), Pantoea disperse (Uniprot: Q6XNK6), Raoultella vegetativea (Uniprot: Q6XKX6), Pseudomonas mesoacidophilus (Uniprot: Q2PS28), Enterobacteriaceae (Uniprot : B5ABD8) and Pectobacter carotovii (Uniprot: S5YEW8). Putative signal peptides of Gram-negative bacteria were predicted by SignalP 4.1 prediction software (Petersen, Nature Methods, 8:785-786, 2011). When present, these signal peptides were replaced by methionine (M), and this resulted in the protein sequences depicted in SEQ ID NO: 1-6.

[0066] Protein sequences (SEQ ID NO: 1-6) were expressed in E. coli as described in WO2017050652(A1). According to DNA2.0 ( Technology) algorithm to codon-optimize a synthetic DNA sequence encoding a putative sucrose isomerase for expression in E. coli. For cloning purposes, a DNA sequence containing an N...

Embodiment 2

[0096] Activity of sucrose isomerase at different pH

[0097] To test the activity of different sucrose isomerases on sucrose at different pH, we incubated 20% sucrose / 250 mM sodium phosphate buffer with 10% dilution (0.07-0.21 mg protein / ml) of different enzymes. The pH of the solution was set at 4.5 and 6.0 and incubated at 37°C for 6 hours before stopping the reaction by heating at 99°C for 5 minutes. The conversion of sucrose to different sugars was quantified using the Dionex HPLC method. The results are shown in Table 3, expressed as the average percentage of experiments obtained from 2-4 different preparations of the corresponding enzyme relative to the total amount of all sugars detected in the samples after incubation.

[0098] Table 3: Conversion of sucrose to various sugars at various pH using sucrose isomerase

[0099]

[0100]

[0101] From Table 3 it is clear that all tested enzymes were able to convert sucrose almost completely at pH 6.0 and pH 4.5. P...

Embodiment 3

[0103] Activity of dextran sucrase at different pH

[0104] To test the activity of different glucansucrases on sucrose at different pH, we incubated 20% sucrose / 250 mM sodium phosphate buffer with 10% dilutions of different enzymes. The pH of the solution was set at 4.5 and 6.0 and incubated at 37°C for 6 hours before stopping the reaction by heating at 99°C for 5 minutes. Sugar composition was quantified using the Dionex HPLC method. The results are shown in Table 4 below, expressed as percentage of total sugars obtained from experiments with corresponding enzymes relative to total sugar after conversion. Because dextran can exist in different forms, it is difficult to quantify using the HPLC method used in these experiments. Therefore, the total glucan formation was calculated from the difference in the increase of fructose and glucose after correcting for the fructose and glucose content of the blank without added enzyme. Therefore, the figures shown are only rough es...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

Sucrose isomerase is used as a nutritional supplement, or can be mixed in with a powderous food / beverage formulation. When an animal, including a human, consumes sucrose, the sucrose isomerase will act on the sucrose present in the food, and will convert the sucrose to other sugars. This results in lowering of the glycemic index of the food without changing the formulation of the food.

Description

technical field [0001] The present invention relates to the use of sucrose isomerase as a nutritional supplement for humans and animals. Sucrose isomerase can enzymatically reduce the amount of sucrose in a food after consumption, and thus lower the glycemic index of the food. Sucrose isomerase supplements are especially beneficial for lowering blood sugar, lowering the glycemic index of foods and / or beverages consumed, and managing or reducing weight. Background technique [0002] Hyperglycemia ranks high in the global burden of disease and can lead to obesity and type 2 diabetes. Foods and beverages that contain rapidly absorbed carbohydrates, such as sugars or starches, can cause a rapid increase in blood sugar followed by a spike in insulin release, causing a rapid decrease in blood sugar. Foods and beverages that lack these carbohydrates result in slower and lower increases in blood sugar and less rapid peak insulin release. This response in blood glucose is expresse...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): A23L33/00A23L33/195A61K38/45A61K38/52
CPCA23K20/189A23K50/40A23L29/06A23L33/10A23L33/195A23L33/30A61K38/52C12Y504/99011A23V2002/00A23V2200/328A23V2200/332A23L33/40A23L2/52
Inventor 马艾克·约翰娜·布鲁因斯彼得吕斯·雅各布斯·西奥多瑞斯·蒂克尔杰伦·阿德里亚努斯·约翰尼斯·努伊彦斯
Owner DSM IP ASSETS BV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com