alpha-amylase and Glucose Oxidase as Promising Improvers for Wheat Bread

Author(s):  
Jie Zeng ◽  
Haiyan Gao ◽  
Guanglei Li ◽  
Xinhong Liang
2016 ◽  
Vol 46 (12) ◽  
pp. 2249-2256 ◽  
Author(s):  
Camila Batista da Silva ◽  
Eveline Lopes Almeida ◽  
Yoon Kil Chang

ABSTRACT: This study aimed to verify the performance of xylanase and its interaction with oxidants agents (glucose oxidase and ascorbic acid) on the quality of whole wheat bread. The experiment was based on a central composite rotational design and the Response Surface Methodology was used to analyze the results. None of the xylanase, glucose oxidase or ascorbic acid concentrations within the studied range led to a significant difference in the specific volume. The highest moisture content and the lowest firmness values were reported in the bread with lower and intermediate levels of xylanase and larger amounts of glucose oxidase and ascorbic acid. This effect was observed mainly at the end of the storage period. A minimum amount of xylanase (from 33 to 63 EDX kg-1 flour) showed to be essential for obtaining best results. Levels of ascorbic acid above 63mg kg-1 and glucose oxidase above 91 SRU kg-1 proved to be necessary to offer the beneficial effect of xylanase.


2011 ◽  
Vol 236-238 ◽  
pp. 35-38
Author(s):  
Jie Zeng ◽  
Hai Yan Gao ◽  
Lei Jin ◽  
Zhao Pei Zhang ◽  
Hui Rong Zhang

The effects of α-amylase and glucose oxidase as bread improvers on the textural properties of bread were evaluated by texture profile analysis and Scanning electron micrograph. It was found that α-amylase and glucose oxidase could retard the bread aging. And Scanning electron microscopy showed that wheat bread with the addition of the enzymes exhibited the microstructures with the smoother surfaces. Therefore, α-amylase and glucose oxidase could be considered as the potential texture modifier for baked food.


1978 ◽  
Vol 24 (8) ◽  
pp. 1393-1398 ◽  
Author(s):  
R C Barabino ◽  
D N Gray ◽  
M H Keyes

Abstract We described a partitioned enzyme-sensor system, which incorporates an immoblized substrate and three or more discrete immobilized enzymes. This instrument measures alpha-amylase activity by passing the solution containing alpha-amylase over a column packed with immobilized starch. The resulting oligosaccharides are successively exposed to a column or columns containing immobolized glucose oxidase, catalase, glucoamylase or maltase, and glucose oxidase. The resulting hydrogen peroxide is detected by a three-electrode amperometric cell. All immobilized reagents were immobilized on a particulate, porous alumina to allow rapid and constant flow rate. With use of less than optimum immobilized reagents, alpha-amylase activity has been measured from about 5 to 200 kU/liter with a 50 microliter sample size. Lack of sensitivity is predominantly attributable to the low activity and low stability of immobilized maltase and glucoamylase. We believe that a clinical test using this system is feasible and desirable because the immobilized reagent system should allow for testing of alpha-amylase with excellent precision, convenience to the operator, and low cost.


2021 ◽  
pp. 101492
Author(s):  
Arzu Ünal ◽  
Asiye Seis Subaşı ◽  
Semra Malkoç ◽  
İjlal Ocak ◽  
S. Elif Korcan ◽  
...  

2013 ◽  
Vol 51 (08) ◽  
Author(s):  
V Zevallos ◽  
P Olinga ◽  
Y Junker ◽  
PB Tung ◽  
N Volz ◽  
...  

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