By the context of application enzymes are often categorized according to the compounds they act upon or technical purposes. Some of the most common enzymes include proteases for protein breakdown, cellulases for cellulose degradation, lipases for lipid hydrolysis and amylase for starch depolymerization, and so on. Very often enzymes are also named by their technical purposes, such as liquefaction enzyme, saccharification enzyme, mashing enzyme. The naming of an enzyme product sometimes indicates some of its characteristics like pH or temperature dependence, for example, acid protease, thermostable alpha-amylase, alkaline protease, etc. The name of an enzyme can very well be connected to its source, such as plant protease, microbial protease, fungal amylase, etc. Sometimes you can hardly find any clue to how an industrial enzyme product is named, because it is the preference of the company producing it or person who is in charge of naming.

Enzyme activity (normally expressed in “u”) is defined as the amount of enzyme preparation needed to convert a specific substrate to produce certain amount of product per unit time. However, this analysis depends on many factors such as substrate used, the temperature, pH, substrate concentration, enzyme concentration, presence of inhibitors and activators, etc. So, it’s very important to specify the exact condition where the enzyme activity is analyzed. As a result, there may be different activity for one enzyme due to different analysis method. 

Specific activity measures the activity of an enzyme on basis of protein content and is the index of enzyme purity. Furthermore, the specific activity of an enzyme also measures the turnover number of the enzyme.

Purity is often used to evaluate the quality of a product. Strictly speaking, enzymatic purity or activity purity refers to the fraction of activity observed in an assay that comes from a single enzyme. Typically, if 100% (or nearly so) of the observed activity in an enzyme assay is derived from a single enzyme, then the enzyme preparation is considered enzymatically pure, even if it lacks mass purity. For quality control a manufacturer may use a standardized method to do activity analysis, and the activity can be regarded as the index for “purity”. Please be noted that the activity values from different manufacturers are incomparable in most cases since the definition of activity unit is different.  

Enzyme activity depends on several factors such as temperature, pH, substrate concentration, enzyme concentration, presence of inhibitors or activators, and other environmental factors.

Temperature is one of the most important factors affecting enzyme activity. Each enzyme has an optimal temperature at which it exhibits maximum activity. This is usually around 37 °C for enzymes found in humans and other mammals. However, enzymes from extremophiles can function at much higher temperatures, up to 100 °C or more. At lower temperatures, enzyme activity decreases due to decreased molecular motion and reduced collision frequency between substrates and enzymes. At higher temperatures, enzyme activity also declines due to denaturation and loss of structure and function.

pH is another critical factor influencing enzyme activity. Each enzyme has an optimal pH range at which it exhibits maximum activity. This is because different enzymes have different acidic or basic functional groups in their active sites that interact with the substrate. Changes in pH can affect the ionization state and hence the reactivity of these groups, thereby altering enzyme activity. For example, pepsin, a digestive enzyme secreted by the stomach, has an optimal pH of 1 to 2, while trypsin, another digestive enzyme secreted by the pancreas, has an optimal pH of 7 to 8.

Substrate concentration is also an important determinant of enzyme activity. The rate of an enzyme-catalyzed reaction increases with increasing substrate concentration until a saturation point is reached. At this point, further increases in substrate concentration do not increase the rate of the reaction but instead result in competition for the limited number of enzyme molecules. Therefore, it is essential to optimize the substrate concentration when measuring enzyme activity to obtain accurate results.

Enzyme concentration is another factor that influences enzyme activity. As the enzyme concentration increases, the rate of the reaction also increases until all available substrate molecules are converted to product. However, beyond this point, further increases in enzyme concentration do not increase the rate of the reaction but instead lead to enzyme inhibition due to depletion of substrate molecules.

Inhibitors and activators can also affect enzyme activity. Inhibitors are compounds that reduce or abolish enzyme activity, while activators enhance enzymatic activity. Some inhibitors bind to the enzyme active site and prevent substrate binding, while others bind to allosteric sites and alter the conformation of the enzyme, thereby affecting its activity. Activators, on the other hand, bind to allosteric sites and induce changes in enzyme conformation that enhance substrate binding and catalysis.

The GMOs are defined as the microbes that have desired changes introduced into genetic material by using genetic techniques. Enzymes are not microorganisms and therefore is not GMO.

Nowadays, most enzymes used in food production worldwide are produced by recombinant DNA techniques, that is, the microorganism or product strain can be a GMO, which brings benefits in production economy in terms of yield, reduce fermentation time and easy processing, etc., improved enzyme properties of better selectivity, more practical pH, temperature, salt concentration, and cofactor requirements.

Despite concerns from some consumers about the safety of GMOs, all microorganisms used for enzyme production have been thoroughly evaluated and approved by regulatory agencies such as the U.S. Food and Drug Administration (FDA) and the European Food Safety Authority (EFSA). These agencies carefully assess the safety of GMOs before they are approved for commercial use, ensuring that they are safe for human consumption and the environment.

Quality of enzyme products is often measured by its declared activities. Therefore, there is a quality parameter called "Declared activities". In the context of industrial application, we focus more on performance than activity, though they are somehow correlated. In industrial application enzymes are used to address certain concerns like yield increase, processing difficulty, stability, and so on. Very often a successful industrial enzyme product contains different enzymes that are necessary to solve specific problem, while only one enzyme or a few activities are declared for one enzyme product in most cases. The complexity in understanding enzyme activity of similar products from different manufacturers is also closely related to the way they use for the activity analysis. Therefore, the declared activities are not necessarily an indication of performance.

Enzymes are proteins that can be sensitive to environmental conditions such as temperature, moisture, light, and microbial attack. Storing enzymes in a cool and dry place helps to protect their structure and activity by slowing down the rate of chemical reactions from causing denaturation or degradation of the enzyme. Normally, microorganisms grow better under moist condition, where enzymes are subjected to higher risk of infection.

Enzymes may also be sensitive to light, particularly ultraviolet (UV) light, which can cause photochemical damage to the protein structure. Longer time contact with air may lead to more microbial infections, which is disastrous to enzymes. Sealing the containers and storing them away from light can help to prevent these types of damage and preserve the activity of the enzyme.

Each enzyme has its specific best condition in which the activity of the enzyme is the highest, while an industrial enzyme preparation often contains more than one enzymes, the performance of the preparation is the results of all enzyme activities in the preparation, and the optimal condition has to be found out by trial and error for a given application using the most relevant parameters. Considering the variations in raw materials, products from different suppliers, processing conditions on different occasions, expectations, and so on, the optimal condition also changes.

YES. The use of enzymes can be dated back to thousands of years ago, when our ancestors used natural fermentation to make wine. It’s the enzymes in microorganisms that were working. Today’s industrial enzymes are produced by modern biotechnology, where production strains have been strictly evaluated for their safety, and production processes are very carefully controlled to ensure the safe use of enzymes.

No. Enzymes are protein extracted from microorganisms that are not live. They are only protein having catalytic capability and will never grow.

There are many ways to classify enzymes. According to Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, enzymes are classified into 6 big groups:

Note: The given examples are just a few of the many enzymes within each class, and their applications are not limited to the mentioned industries.

Industrial enzyme products may seem expensive to customers, but it's important to understand that the cost of enzymes is only a small fraction of the total production cost for many industries. Enzymes are highly efficient and can catalyze chemical reactions at very low concentrations, meaning that even a small amount of enzyme can have a significant impact on product quality and yield. 

For example, in the food industry, enzymes can be used to improve the texture, flavor, and nutritional value of products while reducing processing time and waste. In the textile industry, enzymes can be used to soften and finish fabrics more efficiently and sustainably than traditional methods. In the biofuel industry, enzymes can be used to break down biomass into sugars for fermentation, increasing yields and reducing costs.

By using enzymes, manufacturers can achieve higher yields, reduce processing times, and improve product quality, which can ultimately lead to increased profits. Additionally, enzymes are often more environmentally friendly than traditional chemical processes, as they operate under mild conditions and generate fewer toxic byproducts.

Enzymes can be considered either additives or processing aids, depending on their specific use and function in a food or beverage product.

In general, enzymes that are added to a product as an ingredient to achieve a specific technological function, such as improving texture or flavor, are considered additives. For example, an enzyme that helps break down lactose in milk to make it more easily digestible for people with lactose intolerance would be considered an additive.

On the other hand, enzymes used during the manufacturing process to aid in the production of a food or beverage product, but which are not present in the final product, are considered processing aids. For example, an enzyme used to clarify fruit juice by breaking down pectin would be considered a processing aid, and it's removed or inactivated during processing.

One may find that some enzymes are also available from reagent suppliers but much more expensive than from an industrial enzyme manufacturer. What are their differences?

Reagent enzymes:

- Usually highly purified enzymes with defined molecular structure and specific activity

- Used for mechanistic studies and research purposes

- Often characterized using advanced techniques such as X-ray crystallography and NMR spectroscopy

- Typically more expensive and may not be available in large quantities

- Examples include restriction enzymes, polymerases, and proteases

Industrial enzymes:

- Designed and optimized for practical applications in various industries, such as food, beverage, detergent, and biofuel production

- Produced in large quantities using fermentation or genetic engineering methods

- May have multiple side activities to improve efficiency in complex environments

- Cost-effective and can enhance production efficiency and quality

- Examples include amylases, cellulases, lipases, and proteases

To summarize, reagent enzymes are mainly used for research purposes, while industrial enzymes are designed to solve practical problems in various industries. Reagent enzymes are usually pure and expensive, while industrial enzymes are optimized for specific applications and produced in large quantities at a lower cost.

Sunson is a strong believer in bio-solution, thinking it is the future. Today we are faced with many challenges: the growing population against limited natural resources, fast economic development against more environmental pollution, and more and more diversified needs for a better life. Biotechnology will bring sustainable solutions to these dilemmas. Over more than 20 years Sunson has acquired substantial competencies and are ready to contribute.

Detergent

Detergent pioneered the industrial use of enzymes. Detergent enzymes are selected based on stain composition and their compatibility with other cleaning agents. For example, protease (protein degrading enzyme) and lipase (fat degrading enzyme) are incorporated into detergent powder to help remove protein and lip stains. Often alkali resistant enzyme complex is used to effectively remove the stains on clothes. 

Textile

Enzymes have been widely used to substitute harmful chemicals in many traditional processes. Textile industry exemplifies well the changes:

Bioscouring: Alkaline pectinase is used for Bio-scouring (purifying) natural cellulosic fibres such as cotton, linen, hemp and blends. It removes pectin and other impurities from cotton fibres without any damages to cellulose. Traditionally this was done with very caustic chemicals.

Denim abrasion: small enzyme dosage can replace traditional pumice stones to be used in stonewashing of denim to achieve a worn look

There are far more successful enzymatic applications covering food & baking, brewing, animal feed, alcohol, fruit juice & wine, textile & leather, oil and fats and pulp and paper industries.

Industrial enzymes refer to biological catalysts used on a large scale in various industries, including food and beverage, textile, paper and pulp, detergents, cosmetics, pharmaceuticals, and many more. The development of industrial enzymes involves several steps, starting from identifying the microorganism to the production of the final enzyme product.

The first step in developing industrial enzymes is to identify a microorganism that produces the enzyme of interest. This microorganism is usually identified in nature, isolated and screened for its ability to produce high quantities of the enzyme. Once identified, the microorganism is then bred in the laboratory using traditional or modern biotechnology techniques to improve its production performance. This breeding process may involve genetic modification in some cases.

The selected production strain is then inoculated into well-contained fermentation vessels, which are carefully monitored for optimal growth conditions such as temperature, pH, nutrient availability, and oxygen supply. During fermentation, the production strain converts the raw materials into the desired enzyme product. This process can take several days to weeks, depending on the type of enzyme being produced.

Once the fermentation is complete, the mixture containing the enzyme product is harvested and subjected to various purification techniques to isolate the enzyme from other cellular components. These purification techniques may include filtration, centrifugation, chromatography, and precipitation. The purified enzyme is then formulated into a final product suitable for its intended application.

Formulation of the enzyme product may include blending with other ingredients to stabilize the enzyme, controlling the pH and temperature for optimal activity, and packaging the final product for ease of handling and storage. Quality control measures are also implemented throughout the entire development process to ensure the safety and efficacy of the final product.

Enzymes bring lots of environmental benefits. A few examples are as follows:

•Replace harmful chemicals: substitute acids, alkali or oxidizing agents in fabric de-sizing; Use enzymes in the tanneries to reduce the use of sulfide

•Reduce environmental load: Enzymes used in feed help animals with better digestion and nutrient absorption, making better use of feed while reducing organic substance in manure.

•Reduce energy consumption: Enzymes allow laundry to be done at lower temperature with more efficient cleaning saving electricity consumption.  

•Waste water treatment: enzymes are being used for waste water treatment directly contributing to environment protection.

It’s proven fact that the use of enzymes will reduce appreciable amount of CO₂ emission a lot. 

NO. As said, enzymes are protein and biodegradable. On the contrary, enzymes are ecofriendly solutions since their uses lead to great reduction in energy consumption and much less waste discharge. Even enzymes have been successfully developed to address environmental concerns. 

Like all other catalysts, enzymes promote reactions in a way to allow the reactions to take place in a much milder condition and greatly increase the efficiency. Enzymes are specific. In other words, one category of enzymes only works on one kind of substance. For example, amylase only attacks starch, and protease only digests proteins.