Glucose Oxidase (GOD) 2000 U/g, Aspergillus niger Feed/Food Enzyme Preparationとは？用途・使用量・代替品・規格

Glucose Oxidase (GOD, EC 1.1.3.4, systematic name β-D-glucose oxidoreductase) is an aerobic dehydrogenase that specifically catalyzes the reaction of β-D-glucose with oxygen to produce δ-D-gluconolactone and hydrogen peroxide. Glucose oxidase is an important industrial enzyme in the food industry, widely used for oxygen removal in wine, beer, fruit juice, milk powder and other foods, flour improvement, and prevention of food browning. It is also widely used in food rapid detection and biosensors. In terms of sources, glucose oxidase is widely distributed in animals, plants, and microorganisms. Due to their fast growth and wide availability, microorganisms are the main source of GOD production, with the main producing strains being Aspergillus niger and Penicillium. Commonly used production strains include Aspergillus niger, Penicillium notatum, Penicillium chrysogenum, and recombinant Pichia pastoris. Glucose oxidase is an important oxidoreductase widely used in food, feed, pharmaceutical, textile and other industries. It can be used to improve the digestion and utilization rate of animal feed. Glucose oxidase is non-toxic and has no side effects on the human body, with functions including glucose removal, oxygen removal, and sterilization. It has been widely used in food, feed, pharmaceutical and other industries.

Glucose oxidase is known as the "multifunctional oxidoreductase tool enzyme of the food industry" and the "core enzyme for green biological preservation," occupying a rapidly rising core position in global food processing, feed industry, medical diagnostics, and biosensors. Its most prominent core advantages include: highly specific catalytic properties, green and safe preservation principles, multifunctional application of glucose removal, good temperature and pH applicability, and continuously advancing enzyme engineering technology. 1 Highly specific catalytic properties Glucose oxidase exhibits high specificity for β-D-glucose, with a cross-reactivity rate of ≤2% for interfering substances such as galactose and xylose. Its systematic name is defined as β-D-glucose:oxygen 1-oxidoreductase, capable of specifically oxidizing β-D-glucose to produce δ-gluconolactone and hydrogen peroxide. It requires flavin adenine dinucleotide (FAD) as a coenzyme and is widely used in food rapid detection and biosensors. This specificity makes it irreplaceable in clinical diagnostics and food testing. 2 Green and safe preservation principles Glucose oxidase is a green biological food preservative capable of removing dissolved oxygen from food, providing preservation, color protection, browning prevention, vitamin C protection, and extending food shelf life. Using glucose oxidase can remove oxygen from food and containers, effectively preventing food spoilage, thus it can be applied to packaging of feed, tea, ice cream, milk powder, beer, fruit wine, and other beverage products. As a naturally sourced bio-enzyme, glucose oxidase is non-toxic and has no side effects on the human body at recommended usage levels, aligning with "clean label" and green manufacturing trends. 3 Multifunctional application of glucose removal Glucose oxidase catalyzes the oxidation reaction of D-glucose and can be used to remove glucose from egg liquid to prevent discoloration and deterioration of protein products during storage. In food, glucose oxidase has the functions of converting glucose and removing residual oxygen, preserving the color, aroma, and taste of food, stabilizing product quality, and extending shelf life. In clinical diagnostics, the refined enzyme can be used for rapid and accurate determination of glucose content in body fluids, providing reliable data for doctors to accurately assess patients' conditions. 4 Good temperature and pH applicability Glucose oxidase is active and stable in the pH range of 3.0–8.0, with an active temperature range of 20–65°C. It can function in the pH range of 3.5–6.5 and temperature range of 20–70°C, with optimal temperature 30–40°C and optimal pH 3.5–6.5. The wide adaptability to pH and temperature ranges enables it to meet most food and feed industry processing conditions. The research and application of heat-resistant and acid-resistant glucose oxidase has further solved the defect of low enzyme activity caused by high temperature and acidic environments in food and feed, expanding the application space of glucose oxidase under more rigorous processing conditions. 5 Continuously advancing enzyme engineering technology Enzyme engineering modification technology for glucose oxidase is developing rapidly. The fermentation preparation and separation and purification methods of heat-resistant and acid-resistant glucose oxidase have been patented, solving the defect of low enzyme activity caused by high temperature and acidic environments in food and feed. Important breakthroughs have also been made in the separation, purification, and characterization of recombinant Pichia pastoris glucose oxidase. With the continuous development of genetic engineering, high-density fermentation, and immobilized enzyme technology, the yield, thermal stability, and operational stability of glucose oxidase continue to improve, while production costs continue to decline.