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glucoamylase
JOURNAL OF FOOD BIOCHEMISTRY · 2018 ·Vol. 43 ·期 3 ·e12741 · IF 1.552

Co-immobilization of pectinase and glucoamylase onto sodium aliginate/graphene oxide composite beads and its application in the preparation of pumpkin–hawthorn juice

Si-Qi Yang,Xiao-Yan Dai,Xiao-Yi Wei,Qing Zhu,Tao Zhou

Co-immobilization of pectinase and glucoamylase onto sodium alginate/graphene oxide beads was achieved by N , N′ -dicyclohexylcarbodiimide/ N -hydroxysuccinimide as activating agent. The co-immobilized pectinase-glucoamylase (I-PG) prepared under optimal conditions (pH 4.0, 40°C and 35 min) possessed pectinase activity of 1,227.5 ± 36.5U/g and glucoamylase activity of 1,027.2 ± 29.2U/g, with activity recovery of 73.8% and 85.2%, respectively. Both pectinase and glucoamylase in I-PG possessed wider pH tolerance and superior thermal stability to those of their free counterparts. Reusability studies indicated that both enzymes in I-PG retained over 60% of initial activity after six times of reuse. Conditions for the hydrolysis of the pumpkin–hawthorn compound juice by I-PG were optimized using orthogonal experiments. After treatment with I-PG, light transmittance, soluble solids, and reducing sugar content in the resulting juice increased significantly, whereas soluble protein and pectin content decreased appreciably. Therefore, the use of I-PG provided an effective and feasible method for improving quality of the pumpkin–hawthorn juice. Practical applications In order to overcome the drawbacks of using free pectinase and glucoamylase, an effective method for the co-immobilization of these two enzymes onto sodium alginate/graphene oxide beads was developed. The co-immobilized pectinase/glucoamylase developed in this study could be applied in the clarification of juice rich in pectin and starch.

研究领域: 食品科学与工程 · 酶工程
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PLoS One · 2013 ·Vol. 8 ·期 8 ·e70841 · IF 3.73

The Effect of Polyhydroxylated Alkaloids on Maltase-Glucoamylase

Qian Shang,Junfeng Xiang,Hong Zhang,Qian Li,Yalin Tang

One of the most important carbohydrate-splitting enzymes is themaltase-glucoamylase which catalyzes the hydrolysis of alpha-glucosidic linkages. Maltase-glucoamylase inhibitors during the last few years have aroused medical interests in the treatment of diabetes. They contribute to a better understanding of the mechanism of maltase-glucoamylase. At present there are many different classes of maltase-glucoamylase inhibitors. This paper focuses on alkaloidal inhibitors of maltase-glucoamylase and structure-activity relationship (SAR) studies between them in order to discover some drugs with better efficiency and lower toxicity for treating diabetes.

研究领域: 药理学 · 生物化学
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LWT-FOOD SCIENCE AND TECHNOLOGY · 2024 · IF 6

Investigation of the potential mechanisms of α-amylase and glucoamylase through ultrasound intensification

Yanan Wang,Xuezhi Tian,Zehua Zhang,Meiling Tian,Fusheng Zhang

The aim of this study is to enhance the efficiency of enzymes, reduce operational costs, and increase production output. Experimental research shows that ultrasound positively impacted the activity of α-amylase and glucoamylase, with the peak α-amylase activity observed at 30 W for 5 min and the highest glucoamylase activity at 60 W for 3 min. Ultrasonication extended the optimal temperature of both enzymes, but had no effect on the optimal pH. According to the kinetic experiments, ultrasonic treatment could improve the catalytic efficiency of α-amylase and glucoamylase. Furthermore, the SDS-PAGE results revealed that ultrasound treatment did not alter the molecular weights of the enzymes and their primary structures; The circular dichroism and fluorescence spectroscopy analysis indicated the secondary structural components, especially the α-sheet and the tryptophan fluorescence intensity, were notably affected by ultrasound. The changes in the secondary and tertiary structure of α-amylase and glucoamylase suggest that ultrasonic treatment may enhance their activities. Our findings provide a theoretical basis for the efficient utilization of α-amylase and glucoamylase through understanding the enzyme structure changes after ultrasound.

CAS / MDL: 9001-19-8
研究领域: 生物化学 · 酶学 · 超声技术 · 食品科学
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY · 2025 · IF 6.2

Structural Stabilization and Activity Enhancement of Glucoamylase via the Machine-Learning Technique and Immobilization

Frank Peprah Addai,Xinglin Chen,Hao Zhu,Zongjian Zhen,Feng Lin,Chengxiang Feng,Juan Han,Zhirong Wang,Yun Wang,Yang Zhou

Glucoamylases (GLL) hydrolyze starch to glucose syrup without yielding intermediate oligosaccharides, but their lack of stability under industrial conditions poses a major limiting factor. Using consensus- and ancestral-based machine-learning tools, a functional GLL with six mutations (GLLI73l/T130V/N212V/D238G/N327M/S332P) was constructed that exhibited superior hydrolytic activity relative to the wild-type (WT-GLL). An oxidized multi-walled carbon nanotube (oMW-CNT) was used as a solid support to immobilize the WT-GLL with an immobilization capacity of 211.28 mg/g. The specific activity of mutant GLL-6M and GLL@oMW-CNTII was improved by 2.5-fold and 3.9-fold respectively, with both retaining 64.5% residual activity after incubation at 50 °C for 2 h compared to the WT-GLL with 42.6% activity. GLL and GLL-6M were however completely inactivated at 55 °C in 30 min while oMW-CNTII retained ∼43.1% activity. Our results demonstrate that employing a machine-learning approach for enzyme redesign and immobilization is a practicable alternative for improving enzyme performance and stability for industrial applications.

CAS / MDL: 308068-56-6
研究领域: 生物化学 · 酶工程 · 工业生物技术
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FOOD HYDROCOLLOIDS · 2021 · IF 9.147

Effects of α-amylase and glucoamylase on the characterization and function of maize porous starches

Xiuying Han,Huiliang Wen,Yu Luo,Jun Yang,Wenhao Xiao,Xiaoyao Ji,Jianhua Xie

To overcome the limited surface area of starch and improve the adsorption capacity of starch, porous starch has been widely produced in various fields. In this study, the different enzyme activities of α-amylase (AM), glucoamylase (GAM), and mixed enzyme (ME) were used to prepare different types of porous maize starch, and the microstructure, particle morphology, adsorption, and gelatinization characteristics of the porous starch were studied. Scanning electron microscopy showed porous structures with diverse pore size distribution and pore area depending on the enzyme type and its activities; AM produced the largest holes, GAM produced the deepest holes, and ME produced large and deep holes. Adsorptive capacity was significantly affected by enzymatic modification being greater influenced by GAM. The porous starches had higher relative crystallinity as deduced from X-ray diffraction and Fourier transform infrared spectroscopy . The MA-treated starch had higher solubility whereas swelling capacity, peak viscosity, final viscosity, breakdown, and setback of both treatments were decreased compared to the native starch. The results indicate porous maize starch can provide different functions according to the action pattern of enzymes. The type of enzyme and its enzyme activity can be used to produce the ideal cavity and pore size starch granules , which expands its application scope.

研究领域: 食品科学 · 生物化学
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CARBOHYDRATE POLYMERS · 2017 · IF 4.811

Ultrasound assisted enzymatic hydrolysis of starch catalyzed by glucoamylase: Investigation on starch properties and degradation kinetics

Danli Wang,Xiaobin Ma,Lufeng Yan,Thunthacha Chantapakul,Wenjun Wang,Tian Ding,Xingqan Ye,Donghong Liu

The present work investigates the synergistic impact of glucoamylase and ultrasound on starch hydrolysis. The extent of starch hydrolysis at different reaction parameters (ultrasonic intensity, temperature, reaction time) was analyzed. The hydrolysis extent increased with the reaction time and reached a maximum value under ultrasonic intensity of 7.20   W/mL at 10   min. Ultrasound did not alter the optimum enzymatic temperature but speeded up the thermal inactivation of glucoamylase. The evaluation of enzymatic kinetics and starch degradation kinetics indicated a promotion of the reaction rate and enzyme-substrate affinity. According to the thermodynamic results, sonoenzymolysis reactions require less energy than enzymolysis reactions. The measurement of molecular weight, solubility, thermal properties, and structures of the substrates revealed that sonoenzymolysis reaction generated greater impacts on starch properties. The molecular weight and radii of gyration decreased by 80.19% and 90.05% respectively while the starch solubility improved by 136.50%.

研究领域: 化学工程 · 食品科学 · 生物技术
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