Lexicon of enzymes
We compiled a set of definitions of terms concerning
many and diverse functions of enzymes.
Enzymes comprise amino acids that exist in the natural world;
they are safe, environmentally friendly catalysts.
Enzymes also offer the advantage of saving energy
because they accelerate the speed of chemical reactions
under mild temperature and pressure conditions.
Precisely for this reason, enzymes are
drawing attention from around the world
due to their potential contribution to achieve
a sustainable future.
We hope you will be able to imagine how enzymes could help resolve
the problems we are facing today
A
B
C
D
E
F
G
H
I
J
K
L
M
N
O
P
Q
R
S
T
U
V
W
X
Y
Z
α-amylase
a
In 1833, amylase was discovered as the enzyme responsible for breaking down starch in malt. Subsequent research revealed that amylase consists of multiple enzyme types with different functions. In 1924, R. Kuhn discovered an amylase with a powerful gelatinizing effect in the starch of a liquid extracted from a human pancreas. He named it α-amylase.
These widely used enzymes are primarily applied in the liquefaction step of mizuame (a type of malt syrup) and glucose production, as well as in the manufacture of enzymatically produced dextrins, high-maltose syrup, and baking applications.
Numerous α-amylases have been discovered in microorganisms, animals, and plants. In particular, α-amylases from Bacillus species, which are highly thermostable, are used industrially for starch saccharification.
In the 1980s, a new method of sake production called “liquefaction brewing” was developed. Instead of preparing steamed rice, water and white rice are mixed in a vessel equipped with a stirrer. As the rice absorbs water, thermostable α-amylase is added. The mixture is then heated to the optimum temperature (70–80°C) for enzymatic activity, simultaneously causing the gelatinization of the white rice and the liquefaction of the starch. In traditional Japanese sake production, solid steamed rice is used as the raw material. In “liquefaction brewing,” however, liquefied rice is used because its excellent fluidity makes it easier to homogenize the mash through stirring. This enables precise temperature control during fermentation, allowing for the production of high-quality sake.
Numerous α-amylases have been discovered in microorganisms, animals, and plants. In particular, α-amylases from Bacillus species, which are highly thermostable, are used industrially for starch saccharification.
In the 1980s, a new method of sake production called “liquefaction brewing” was developed. Instead of preparing steamed rice, water and white rice are mixed in a vessel equipped with a stirrer. As the rice absorbs water, thermostable α-amylase is added. The mixture is then heated to the optimum temperature (70–80°C) for enzymatic activity, simultaneously causing the gelatinization of the white rice and the liquefaction of the starch. In traditional Japanese sake production, solid steamed rice is used as the raw material. In “liquefaction brewing,” however, liquefied rice is used because its excellent fluidity makes it easier to homogenize the mash through stirring. This enables precise temperature control during fermentation, allowing for the production of high-quality sake.
α-amylases are endo-amylases that randomly cleave α-1,4 glycosidic linkages in the glucose chains of starch, glycogen, and other substances. They are also known as liquefying enzymes. α-amylases hydrolyze starch and other polysaccharides to produce oligosaccharides and dextrins.
α-glucosidase
a
The production of α-glucosidase derived from yeast was first reported by H. Halvorson et al. in 1958. The presence of the enzyme in animal tissues was first reported by A. Dahlquist et al. in 1960, while its presence in insects was first reported by R. E. Huber et al. in 1973.
At least five types of α-glucosidase have been identified in humans, and they are known to function as digestive enzymes. These enzymes are known to catalyze transglycosylation under high substrate concentration conditions and are used in the industrial production of oligosaccharides. α-glucosidases have been reported to enhance the texture of cooked rice, making it fluffier, and are used as rice cooking improvers.
In the medical field, α-glucosidase inhibitors have been commercialized. A diabetes drug has been developed to prevent blood sugar spikes by inhibiting the breakdown of disaccharides into monosaccharides, thereby reducing their absorption in the body. Spices such as allspice, nutmeg, sage, and thyme are also known to have an inhibitory effect on α-glucosidase.
In the medical field, α-glucosidase inhibitors have been commercialized. A diabetes drug has been developed to prevent blood sugar spikes by inhibiting the breakdown of disaccharides into monosaccharides, thereby reducing their absorption in the body. Spices such as allspice, nutmeg, sage, and thyme are also known to have an inhibitory effect on α-glucosidase.
Glycosidase is a general term for enzymes that break down glycosidic bonds in sugars, including glucose. It can also refer to a specific enzyme that catalyzes the breakdown of glycosidic bonds. α-glucosidase is an enzyme that hydrolyzes α-1,4-glycosidic bonds in sugars. This enzyme is present in most living organisms and plays a crucial role in energy production within the body. Since this enzyme catalyzes the hydrolysis of maltose, it is also known as maltase.
Aminoacylase
a
In 1952, Birnbaum et al. of the National Cancer Institute confirmed acylase activity in porcine kidney extract.
A well-known industrial application of this enzyme is the production of L-amino acids. When chemically synthesized N-acyl-DL-amino acids are hydrolyzed by this enzyme, only L-amino acids are produced as decomposition products. This is an excellent method for producing L-amino acids with higher optical purity than other manufacturing processes. The use of immobilized enzyme in this method, studied in 1969, is known as the world’s first industrial application of an immobilized enzyme bioreactor.
Acylase, also known as aminoacylase or N-acyl-L-amino-acid amidohydrolase, is an enzyme that catalyzes the hydrolysis of N-acetylated amino acids into free amino acids and acetic acid. This enzyme is responsible for breaking down acetylated amino acids generated during the decomposition of proteins in cells. This ability suggests that this enzyme could serve as a biomarker for long-term outcomes after kidney transplantation and may play a role in suppressing kidney and liver cell cancers.
Aminoacylase is widely found in animals, plants, and microorganisms. Aminoacylases derived from various organisms have been purified and analyzed to elucidate their enzymatic properties.
Aminoacylase is widely found in animals, plants, and microorganisms. Aminoacylases derived from various organisms have been purified and analyzed to elucidate their enzymatic properties.
Amylase
a
In 1833, French chemists A. Payen and J. Persoz were the first to extract amylase from malt and identify it as the component that breaks down starch. They named it diastase. This was the first time an enzyme was isolated. The enzyme was named amylase after the rules for naming enzymes were proposed in 1898. In 1894, Jokichi Takamine developed the wheat bran-based koji fermentation method for producing amylase using koji mold. He also introduced Taka-Diastase, a digestive enzyme supplement.
Amylases are used for a wide variety of purposes, including starch saccharification, food processing, and brewing; as industrial desizing agents; and as digestive agents in pharmaceuticals.
Koji mold (Aspergillus oryzae), which is highly productive in amylase production, is used as seed koji (fermentation starter), known as moyashi, in the brewing of Japanese sake. Moyashi is made by allowing koji mold to grow on steamed rice coated with wood ash, and then drying the spores. It is believed that dealers specializing in seed koji existed in Japan as early as the Heian period (794-1185).
Koji mold (Aspergillus oryzae), which is highly productive in amylase production, is used as seed koji (fermentation starter), known as moyashi, in the brewing of Japanese sake. Moyashi is made by allowing koji mold to grow on steamed rice coated with wood ash, and then drying the spores. It is believed that dealers specializing in seed koji existed in Japan as early as the Heian period (794-1185).
Amylase is an enzyme that breaks down starch, a type of carbohydrate, into sugars. Amylases are widely found in animals, plants, and microorganisms. In humans, they are mainly secreted by the pancreas, salivary glands, and parotid glands. They are classified into endo-amylases and exo-amylases based on their mode of action. Starch consists of chains of glucose molecules. Endo-amylases cleave bonds within the chains, while exo-amylases break them down from the ends. In human digestion, the two kinds of amylase work together to efficiently break down starch into energy.
β-amylase
b
In 1833, amylase was discovered as the enzyme responsible for breaking down starch from malt. Subsequent research revealed that amylase consists of multiple enzyme types with different functions. In 1924, R. Kuhn discovered an amylase with powerful saccharification action in malt. He named it β-amylase.
β-amylase is present naturally in sweet potatoes, barley, wheat, and soybeans. The enzyme is known to be widely found in higher plants. It was not until the 1970s that industrially useful enzymes derived from microorganisms were discovered.
β-amylase is an exo-type amylase that breaks down the α-1,4 glycosidic linkages to release maltose units from the non-reducing ends of starch, a polymer made up of glucose linked into chains. Starch is composed of amylose, polymerized in unbranched chains with α-1,4-glucosidic linkages, and amylopectin, branched with α-1,6-glucosidic linkages. This enzyme breaks down almost 100% of amylose into maltose. However, the reaction stops before α-1,6 bonds are formed in starch, resulting in the formation of large dextrin molecules. When maltose is produced directly from starch using only β-amylase, the maltose content is around 40%. However, if this enzyme is applied after the starch is broken down with α-amylase, maltose content increases to around 55%.
β-galactosidase
b
β-galactosidase was first reported by M. W. Beijerinck of Delft University of Technology in the Netherlands in 1889 from a microzymic culture (a liquid mixture of bacteria and enzymes) derived from yeast. However, this finding was later refuted. In 1894, β-galactosidase was “rediscovered” by E. Fischer.
It is one of the most important enzymes in the food industry. It can be used to break down lactose in milk and dairy products to enhance sweetness without the addition of sugar and to prevent the deterioration of ice cream texture by inhibiting lactose recrystallization. β-galactosidase is also used to manufacture galacto-oligosaccharides (GOSs) through transglycosylation of lactose. GOSs are functional oligosaccharides that increase the number of bifidobacteria in the digestive tract, with reportedly beneficial effects on the regulation of intestinal functions. GOSs have been certified as a Food for Specified Health Uses (FOSHU) in Japan. GOSs are resistant to both heat and acidity, enabling their use in a wide variety of foods.
β-galactosidase is an enzyme that breaks down lactose, which consists of β-1,4-linked galactose and glucose, into galactose and glucose. This enzyme is also called lactase because it breaks down lactose.
β-galactosidase is widely found in nature. It has been isolated from many different sources, including plants, animals, and microorganisms.
β-galactosidase is widely found in nature. It has been isolated from many different sources, including plants, animals, and microorganisms.
β-glucosidase
b
The first report of this enzyme, found in almond seeds, was published by the German chemist J. Liebig in 1837.
It is thought that β-glucosidase enzymes found in small intestinal mucosa help to break down plant-derived glycosides in food. Isoflavones in soybeans are considered to have health-promoting functions. In processed soybean foods, however, isoflavones are present as glycosides bound to glucose through β-glucosidic bonds. It is thought that these enzymes in small intestine mucosa help to release and absorb the isoflavones in soy foods.
A genetic disorder in humans called Gaucher’s disease is attributed to a congenital deficiency of β-glucosidase. Gaucher’s disease is caused by the absence of a type of β-glucosidase called glucocerebrosidase. Enzyme replacement therapy with glucocerebrosidase has been developed to treat the disease.
A genetic disorder in humans called Gaucher’s disease is attributed to a congenital deficiency of β-glucosidase. Gaucher’s disease is caused by the absence of a type of β-glucosidase called glucocerebrosidase. Enzyme replacement therapy with glucocerebrosidase has been developed to treat the disease.
β-glucosidase is an enzyme that hydrolyzes the β-glycosidic linkages of sugars. It is found in a wide variety of sources, including microorganisms and higher plants; the liver, kidney, and small intestinal mucosa of animals; and the gastric juice of snails. However, its substrate specificity varies depending on its origin.
Chitinase
c
In 1911, French botanist Noël Bernard reported on an enzyme found in an antifungal active compound extracted from orchid bulbs. This was the first report on chitinase in the world.
Chitin is also a component of the cell walls of molds and mushrooms. For this reason, scientists are exploring the potential of chitinases as enzymatic pesticides to inhibit the growth of insects and molds that cause crop damage. In fact, certain actinomycetes in soil secrete chitinase, which dissolves the cell walls of plant pathogens such as Fusarium and other fungi, preventing their growth. It is also known that crab shells and chitosan are used to promote the growth of these actinomycetes. In humans, this enzyme is believed to play a role in biological defense mechanisms.
Glucosamine, produced by the enzymatic breakdown of chitosan by chitinase, is expected to be a valuable ingredient in health supplements. Supplementing with glucosamine is believed to help relieve joint pain by slowing cartilage wear and improving joint mobility. Empirical studies exploring these effects are currently underway.
Glucosamine, produced by the enzymatic breakdown of chitosan by chitinase, is expected to be a valuable ingredient in health supplements. Supplementing with glucosamine is believed to help relieve joint pain by slowing cartilage wear and improving joint mobility. Empirical studies exploring these effects are currently underway.
Chitinases are hydrolytic enzymes that break down the glycosidic bonds in chitin. Chitin, a long-chain polymer of N-acetylglucosamine, is the primary component of the exoskeletons (shells) of crustaceans (e.g., shrimp and crabs) and insects. Chitinases have been found in insects, crustaceans, and fungi, as well as in microorganisms, plants, and animals.
D-Aminoacylase
d
The discovery of D-aminoacylase from the actinomycete Streptomyces olivaceus was reported in 1978. Subsequently, research on the isolation of D-aminoacylase from Pseudomonas and Alcaligenes species was also pursued.
D-methionine and D-phenylalanine are two D-amino acids that are used as ingredients in the production of antibiotics and other active pharmaceutical ingredients (APIs).
Reportedly, D-amino acids play a role in higher brain functions such as memory and learning, as well as in conditions such as schizophrenia and Alzheimer’s. Their involvement in physiological functions and diseases is therefore drawing considerable attention.
Since D-amino acids are likely to be utilized in the development of many drugs in the coming years, the use of D-aminoacylase for synthesizing D-amino acids is expected to become increasingly important.
Reportedly, D-amino acids play a role in higher brain functions such as memory and learning, as well as in conditions such as schizophrenia and Alzheimer’s. Their involvement in physiological functions and diseases is therefore drawing considerable attention.
Since D-amino acids are likely to be utilized in the development of many drugs in the coming years, the use of D-aminoacylase for synthesizing D-amino acids is expected to become increasingly important.
D-aminoacylase was developed as a useful enzyme for the optical resolution production of D-amino acids in the field of synthetic chemistry. D-aminoacylase is known as a hydrolase. By acting on N-acyl (D, L) amino acids, it can selectively synthesize D-amino acids.
D-aminoacylase exhibits excellent stereoselectivity because it reacts specifically with D-amino acids and not with L-amino acids.
D-aminoacylase exhibits excellent stereoselectivity because it reacts specifically with D-amino acids and not with L-amino acids.
Enzymes for yeast extraction
e
The development of yeast extracts for seasoning applications dates back to the early 1900s, though they did not reach the market until the 1950s. Initially, the autolysis method was used with the endogenous enzymes in yeast, but over time, exogenous enzymes such as nuclease and deaminase were introduced to enhance flavor compounds and differentiate products.
The nuclease and deaminase function to convert the nucleic acids from the yeast to 5’-inosinic acid (associated with the umami of dried bonito) and 5’-guanylic acid (associated with the umami of shiitake), thereby enhancing the umami flavor.
Yeast extracts manufactured in this way are widely used in processed foods such as noodle sauces, ramen soups, and instant foods. They are cheaper than chemical seasonings and make it easier to create a distinctive flavor.
Some yeast extracts are also sold as dietary supplements.
Yeast extracts manufactured in this way are widely used in processed foods such as noodle sauces, ramen soups, and instant foods. They are cheaper than chemical seasonings and make it easier to create a distinctive flavor.
Some yeast extracts are also sold as dietary supplements.
When yeast extract is manufactured from beer yeast or baker’s yeast, the enzymes nuclease and deaminase are sometimes used to increase the content of flavor-enhancing nucleic acids, 5’-inosinic acid and 5’-guanylic acid.
Esterase
e
The discovery of lipase, a type of esterase, dates back to pioneering research by the French physiologist C. Bernard in 1844. This is considered the first discovery of an esterase.
Esterases are also attracting attention for their use in breaking down chemical substances for waste disposal. Many new ester compounds have been developed over the years, some of which are used in polymer products such as PET bottles. Since these polymer materials do not naturally break down easily, esterases that accelerate their decomposition are under development The development of esterase applications for producing new chemical substances and breaking down waste materials is expected to continue.
Esterase is a generic term for enzymes that catalyze the hydrolysis of esters. These enzymes are widely found in animal and plant tissues, where they break down esters into acids and alcohols. (* Lipase is a type of esterase that hydrolyzes esters of glycerol and fatty acids, which make up fats and oils.) Many proteases also exhibit esterase activity because the hydrolysis of ester bonds is very similar to the reaction by which proteases break down peptide (amide) bonds.
This hydrolytic enzyme has attracted attention for its applications in chemical synthesis for the production of optically active organic compounds. Compared to chemical methods that do not use enzymes, the high substrate specificity of this type of enzymes results in fewer by-products. For this reason, this method is likely to become more established as a superior process.
This hydrolytic enzyme has attracted attention for its applications in chemical synthesis for the production of optically active organic compounds. Compared to chemical methods that do not use enzymes, the high substrate specificity of this type of enzymes results in fewer by-products. For this reason, this method is likely to become more established as a superior process.
Glucanase
g
In enzyme classification, glucanases include amylases and cellulases, so their discovery dates back to the identification of these enzymes (amylase in 1833, cellulase in 1911).
β-glucan is widely recognized as a natural component of the cell walls of bacteria, fungi, yeasts, and grains such as oats and barley. β-glucanase enzymes, which break down β-glucan, dissolve the cell wall components of filamentous fungi, yeasts, and bacteria. Because of this, they are considered to have potential applications in the prevention and treatment of plant diseases. Industrial applications include producing yeast extract, improving filtration efficiency in beer brewing, and enhancing the digestibility of livestock feed.
Glucanase is a general term for enzymes that hydrolyze glucan, a polysaccharide composed of glucose, to produce gluco-oligosaccharides or glucose. Glucans are classified into two types: α-glucans and β-glucans. The enzyme that breaks down pullulan, a typical α-glucan, is a glucanase called pullulanase.
Glucoamylase
g
This enzyme was discovered in 1949 by Kakuo Kitahara of the Institute for Food Science, Kyoto University.
Due to their ability to produce glucose directly from starch, glucoamylases are industrially valuable enzymes. They are widely used in glucose production, brewing, and other applications. Glucoamylases derived from Rhizopus fungi are used in non-cooking (cold) fermentation methods because they work efficiently without the need to cook the starch.
Japan has been a global leader in the research and development of glucoamylases. The history of this development is said to have been spurred by comparisons between the mechanisms of malt-based saccharification in the West and koji-based saccharification in Japan and other parts of Easts Asia. A world-class biotechnology of carbohydrates developed around these enzymes in Japan. An industrial method for producing glucose from starch saccharification using α-amylases and glucoamylases was developed (1959).
Japan has been a global leader in the research and development of glucoamylases. The history of this development is said to have been spurred by comparisons between the mechanisms of malt-based saccharification in the West and koji-based saccharification in Japan and other parts of Easts Asia. A world-class biotechnology of carbohydrates developed around these enzymes in Japan. An industrial method for producing glucose from starch saccharification using α-amylases and glucoamylases was developed (1959).
Glucoamylases are a type of amylase that sequentially break α-1,4 glycosidic bonds from the non-reducing ends of starch polymers, releasing glucose units. Since they also hydrolyze α-1,6 linkages in amylopectin, some glucoamylases can convert nearly 100% of starch into glucose. These enzymes are commonly found in filamentous fungi but are not found in plants or animals.
Glucose dehydrogenase
g
The discovery of glucose dehydrogenase from microorganisms (Aspergillus) dates back to 1937. This enzyme was first reported by Japanese researcher Y. Ogura et al.
Industrially, glucose dehydrogenase is used mainly as an alternative to glucose oxidase in blood glucose sensors. Glucose oxidase has the advantage of high substrate specificity for glucose, but it is affected by dissolved oxygen, which can lead to measurement inaccuracies. Glucose dehydrogenase has excellent properties for blood glucose sensing because it does not exchange electrons with dissolved oxygen during glucose oxidation. However, its specificity for glucose is lower than that of glucose oxidase, prompting the development of new enzymes for this application.
Glucose dehydrogenase is an enzyme that acts on glucose via an electron donor to convert it into glucono-δ-lactone. However, unlike glucose oxidase, it does not produce hydrogen peroxide.
This enzyme is found in the livers of mammals (e.g., cattle, sheep, dogs, cats), where it is believed to function as a nutrient sensor and a survival-promoting factor. Glucose dehydrogenase has also been found in microorganisms. Enzymes derived from these microorganisms are used for industrial applications.
This enzyme is found in the livers of mammals (e.g., cattle, sheep, dogs, cats), where it is believed to function as a nutrient sensor and a survival-promoting factor. Glucose dehydrogenase has also been found in microorganisms. Enzymes derived from these microorganisms are used for industrial applications.
Glucose Oxidase
g
Glucose oxidase was first identified as an antibacterial agent in Aspergillus niger and Penicillium glaucum by Detlev Müller, a botanist at the University of Copenhagen. Subsequent research found that the antibacterial activity was only expressed in the presence of glucose. The identification of glucose oxidase as the active component was reported in 1928. In 1949, glucose oxidase was confirmed to be an enzyme that converts glucose into gluconic acid in the presence of oxygen.
These enzymes are widely used in food production and as diagnostic agents. In food applications, they are mainly used for eliminating oxygen and glucose.
In diagnostic applications, their high specificity for glucose is utilized for blood sugar quantification. A notable example is the widespread use of simple self-monitoring blood glucose meters that employ electrochemical biosensors consisting of electrodes and an enzyme reaction layer on an insulating substrate. These devices are commonly used by diabetics for self-monitoring of blood glucose.
In diagnostic applications, their high specificity for glucose is utilized for blood sugar quantification. A notable example is the widespread use of simple self-monitoring blood glucose meters that employ electrochemical biosensors consisting of electrodes and an enzyme reaction layer on an insulating substrate. These devices are commonly used by diabetics for self-monitoring of blood glucose.
Glucose oxidase is an enzyme that oxidizes glucose and converts it into glucono-δ-lactone and hydrogen peroxide. Glucose oxidase enzymes have been found in a variety of microorganisms. Outside of microorganisms, this enzyme has also been found in the pharyngeal glands of honeybees. It is present in honey, acting as a natural preservative. This occurs because glucose oxidase, in the presence of glucose on the surface of honey, reduces oxygen in the air to hydrogen peroxide, which acts as an antibacterial agent.
Glycosidase
g
The discovery of glycosidase is attributed to the German chemist J. Liebig, who isolated emulsin (a mixture of enzymes) from almond seeds in 1837. Later research revealed that the principal component of emulsin is β-galactosidase, a type of β-glucosidase.
In the plant tissues of leaves, flowers, and fruits, volatile aromatic compounds bind to sugars through glycosidic bonds, forming non-volatile glycosides that are stored within the plant. During ripening and fermentation, these glycosides are broken down by glycosidase enzymes, releasing the aromatic compounds. The distinctive aromas of fermented teas such as oolong and black tea result from the enzymatic breakdown of glycosides, which releases aromatic compounds.
Glycosidase is a general term for enzymes that hydrolyze glycosidic bonds. These enzymes are found in all living organisms. Both intracellular and extracellular forms of glycosidase are known. Carbohydrates in nature exist in the form of sugar molecules linked to each other or to other organic compounds through glycosidic bonds. This enzyme is therefore generally believed to play a role in nutrient absorption.
Lipase
l
Lipase was discovered in the course of physiology research. In 1844, French physiologist C. Bernard found that pancreatic juice breaks down fats into fatty acids and glycerol, thereby hypothesizing the presence of lipase. In 1896, French physiologist M. Hanriot identified a substance in the blood that breaks down monobutyrin. He named it lipase.
In addition to breaking down fatty acid esters of glycerol, lipases can also facilitate the synthesis of fatty acid esters and catalyze exchange reactions, including reverse reactions. Such reverse reactions are utilized in processes for reforming fats and oils and for producing industrial feedstocks. In such applications, the reactions may occur in organic solvents, requiring enzymes to be resistant to organic solvents. Other known applications of lipases include their use as additives in digestive drugs and detergents.
Lipase in the blood is also used as a biomarker for diagnosing diseases. Patients with pancreatic diseases such as acute pancreatitis, chronic pancreatitis, pancreatic cancer, and pancreatic cysts have elevated levels of lipase in their blood. Measuring blood lipase levels is particularly vital for the diagnosis of acute pancreatitis, which can be fatal if detected too late.
Lipase in the blood is also used as a biomarker for diagnosing diseases. Patients with pancreatic diseases such as acute pancreatitis, chronic pancreatitis, pancreatic cancer, and pancreatic cysts have elevated levels of lipase in their blood. Measuring blood lipase levels is particularly vital for the diagnosis of acute pancreatitis, which can be fatal if detected too late.
Lipases are enzymes that hydrolyze lipids. The term lipase is used particularly to refer to triglyceride lipase, which catalyzes the breakdown of triglycerides (fatty acid esters of glycerol) and releases fatty acids. Triglycerides are a key component of the human diet, as edible fats and oils. Lipase is a digestive enzyme responsible for breaking down lipids in digestive juice (pancreatic juice). Lipases catalyze lipid breakdown in the cells of many types of organisms.
The word “lipase” is derived from the Greek word “lipos,” meaning fat, combined with “ase,” which comes from the enzyme diastase, the first enzyme ever discovered.
The word “lipase” is derived from the Greek word “lipos,” meaning fat, combined with “ase,” which comes from the enzyme diastase, the first enzyme ever discovered.
Protease
p
The first protease ever identified is considered to be pepsin, discovered in gastric juice by the Italian scientist L. Spallanzani in 1783. In an experiment, Spallanzani poured his own gastric juice over beef and observed that it contained enzymes capable of breaking down proteins. In 1825, this enzyme was named pepsin by the German scientist T. Schwann. Systematic research on proteases is thought to have begun in 1907.
Proteases are found in a wide range of organisms, including animals, plants, and microorganisms. In animals, they are recognized as one of the three major digestive enzymes responsible for breaking down meat. It is also well known that microorganisms such as Aspergillus oryzae (koji mold), used to make Japanese sake, and Bacillus subtilis var. natto, used to make natto (fermented soybeans), produce proteases.
Proteases have a wide range of applications, including the production of fermented foods and beverages such as sake and natto, seasonings such as amino acid extracts, and industrial feedstocks such as active ingredients for pharmaceuticals. Proteases are also sold as meat tenderizers. Although proteases are primarily considered enzymes for decomposition, they are also used for the opposite purpose. For example, the coagulation of milk proteins in cheesemaking processes is also due to the action of protease. Cheese is produced when milk proteins are partially broken down by proteases, causing them to coagulate into large solid lumps. The solidified curds are then separated from the liquid to form cheese.
Proteases have a wide range of applications, including the production of fermented foods and beverages such as sake and natto, seasonings such as amino acid extracts, and industrial feedstocks such as active ingredients for pharmaceuticals. Proteases are also sold as meat tenderizers. Although proteases are primarily considered enzymes for decomposition, they are also used for the opposite purpose. For example, the coagulation of milk proteins in cheesemaking processes is also due to the action of protease. Cheese is produced when milk proteins are partially broken down by proteases, causing them to coagulate into large solid lumps. The solidified curds are then separated from the liquid to form cheese.
Proteases are enzymes that hydrolyze proteins and polypeptides. There are two types of proteases: one type selectively cleaves specific sequences of amino acids within proteins or polypeptides composed of various amino acids (high substrate specificity), while the other type cleaves with little specificity (low substrate specificity).
Xylanase
x
The first known report on xylanase is believed to have been published by R. Whistler et al. in 1955 in the U.S. (J. Am. Chem. Soc. 77, 1241–1243).
Xylanases are used to improve the workability of bread dough, as well as to enhance the extraction of coffee and vegetable oils, and the digestibility of silage and cereals. They are also used in the paper industry for the chlorine-free bleaching of wood pulp.
The improvement of xylanase, along with cellulase, for bioethanol production, which has been a hot topic in recent years, has been studied extensively. Much of this research focuses on discovering new enzymes and enhancing them through protein engineering.
The improvement of xylanase, along with cellulase, for bioethanol production, which has been a hot topic in recent years, has been studied extensively. Much of this research focuses on discovering new enzymes and enhancing them through protein engineering.
Xylanases are enzymes that break down xylan into xylose. Xylan is a polymer composed of β-1,4-linked D-xylose molecules. Along with lignin and cellulose, it forms hemicellulose, a key component of cell walls. Xylanase therefore promotes the decomposition of cell walls. This enzyme is found in microorganisms that utilize plant matter as a nutrient source for growth. It is not present in mammals or other animals.