FastEnzymes

CLINICAL STUDIES ON THE FOLLOWING INGREDIENTS:

Lipase

Biochemistry, Lipase

INTRODUCTION Lipases are a family of enzymes that break down triglycerides into free fatty acids and glycerol. There are expressed and active in multiple tissues; for example, hepatic lipases are in the liver, hormone-sensitive lipases are in adipocytes, lipoprotein lipase is in the vascular endothelial surface, and pancreatic lipase is in the small intestine. Lipases in pancreatic secretions are responsible for digestion and hydrolysis of fat and absorption of fat-soluble vitamins. Understanding the lipase function is crucial for the pathophysiology of fat necrosis and acute and chronic pancreatitis. Also, lipases play an essential role in the mechanism of some cholesterol-lowering medications. This review will explore the lipase enzyme's function, pathophysiology, and clinical significance.

MOLECULAR The lipases belong to the alpha/beta-hydrolase fold superfamily of enzymes. They work by employing chymotrypsin-like hydrolysis, which uses a histidine base, a serine nucleophile, and aspartic acid.

FUNCTION Lipase is an enzyme that breaks down triglycerides into free fatty acids and glycerol by catalyzing the hydrolysis of the ester bonds in triglycerides. Lipases are present in pancreatic secretions and participate in fat digestion and metabolism. They play an essential role in lipid transport and serve individual functions in several tissues, including hepatic lipase in the liver, hormone-sensitive lipases in the adipocytes, lipoprotein lipase in the endothelial cells, and pancreatic lipase in the small intestine. Hepatic lipase in the liver degrades the triglycerides that remain in intermediate-density lipoprotein (IDL). Hormone-sensitive lipase is found within fat tissue and is responsible for hydrolyzing the triglycerides stored within adipocytes. Lipoprotein lipase is found in the vascular endothelial cells and is responsible for degrading triglycerides that circulate from chylomicrons and very low-density lipoproteins (VLDLs). Pancreatic lipase is found within the small intestine and is involved in degrading dietary triglycerides.
The LDL ultimately serves to transport cholesterol from the liver to peripheral tissue. Hepatic lipase plays a crucial role in developing and delivering low-density lipoprotein (LDL). The LDL is formed by modifying the IDL in the peripheral tissue and liver by hepatic lipase. These LDL particles are taken up, or endocytosed, via receptor-mediated endocytosis by target cell tissue. The LDL ultimately serves to transport cholesterol from the liver to peripheral tissue.

Source: Yasaman Pirahanchi and Sandeep Sharma. “Biochemistry, Lipase” StatPearls (2022).

Lactase

Lactose Intolerance

CONTINUING EDUCATION ACTIVITY Lactose intolerance is a clinical syndrome that manifests with characteristic signs and symptoms upon consuming food substances containing lactose, a disaccharide. Normally upon lactose consumption, it is hydrolyzed into glucose and galactose by the lactase enzyme, which is found in the small intestinal brush border. Deficiency of lactase due to primary or secondary causes results in clinical symptoms. This activity describes the pathophysiology of lactose intolerance and highlights the role of the interprofessional team in its management.

Objectives:

• Review the pathophysiology of lactose intolerance.
• Describe the presentation of a patient with lactose intolerance.
• Summarize the management options for lactose intolerance.
• Outline the importance of improving care coordination among interprofessional team members to improve outcomes for patients affected by lactose intolerance.

INTRODUCTION Lactose intolerance is a clinical syndrome that manifests with characteristic signs and symptoms upon consuming food substances containing lactose, a disaccharide. Normally upon lactose consumption, it is hydrolyzed into glucose and galactose by the lactase enzyme, which is found in the small intestinal brush border. Deficiency of lactase due to primary or secondary causes results in clinical symptoms. Disease severity varies among individuals. Lactose is present in dairy, milk products, and mammalian milk. It is also sometimes referred to as lactose malabsorption.
Lactase deficiency is the commonest type of disaccharidase deficiency. Enzyme levels are at the peak shortly after birth and decline after that, despite continued lactose intake. Among the animal world, nonhuman mammals generally lose their ability to digest lactose into its components as they reach adulthood. Certain populations of the human species, such as those of South American, Asian, and African descent, tend to develop lactase deficiency. On the contrary, people of northern Europe origin or northwestern India usually retain the ability to digest lactose into adulthood.
Lactose intolerance presents with abdominal bloating and pain, loose stools, nausea, flatulence, and borborygmi. Many people start avoiding milk as soon as a diagnosis is made, or even the suggestion of lactose intolerance is put forward. This leads to consuming specially prepared products with digestive aids, adding to the health care burden.

ETIOLOGY Lactase enzyme deficiency can occur in individuals with lower levels of this enzyme, resulting in failure to hydrolyze lactose into absorbable glucose and galactose components. There are four leading causes of lactase deficiency.
Primary Lactase Deficiency It is the most common cause of lactase deficiency, also known as lactase non-persistence. There is a gradual decline in lactase enzyme activity with increasing age. Enzyme activity begins to decline in infancy, and symptoms manifest in adolescence or early adulthood. More recently, it has been observed that lactase non-persistence is of the ancestral form (normal Mendelian inheritance), and lactase persistence is secondary to mutation.
Secondary Lactase Deficiency Due to several infectious, inflammatory, or other diseases, injury to intestinal mucosa can cause secondary lactase deficiency. Common causes include:

• Gastroenteritis
• Celiac disease
• Crohn disease
• Ulcerative colitis
• Chemotherapy
• Antibiotics

Congenital Lactase Deficiency There is a decrease or absence of lactase enzyme activity since birth due to autosomal recessive inheritance. It manifests in the newborn after ingestion of milk. It is a rare cause of the deficiency, and its genetics are not very well known.
Developmental Lactase Deficiency It is seen in premature infants born at 28 to 37 weeks of gestation. The infant's intestine is underdeveloped, resulting in an inability to hydrolyze lactose. This condition improves with increasing age due to the maturation of the intestine, which results in adequate lactase activity.

Source: Talia F. Malik and Kiran K. Panuganti. “Lactose Intolerance” StatPearls (2022).

Cellulase

Microbial Cellulases: An Overview and Applications

Abstract

Cellulases are a complex group of enzymes which are secreted by a broad range of microorganisms including fungi, bacteria, and actinomycetes. In the natural environment, synergistic interactions among cellulolytic microorganisms play an important role in the hydrolysis of lignocellulosic polymer materials. In fact, it is the combined action of three major enzymes which determines the efficiency of this process. They are exoglucanases, endoglucanases, and β-glucosidase. Microorganisms produce these enzymes in a diverse nature which determines their efficiency in cellulose hydrolysis. During the cellulose degradation reaction, the enzyme targets the β-1,4-linkages in its polymeric structure. This is an essential ecological process as it recycles cellulose in the biosphere. The application of this same scenario for industrial purposes is identified as an emerging area of research. Biofuel production, textile polishing and finishing, paper and pulp industry, and lifestyle agriculture are among the key areas where cellulase enzyme shows a broader potential. The objective of this chapter is to discuss the structure, function, possible applications, as well as novel biotechnological trends of cellulase enzymes. Furthermore, possible low-cost, enzymatic pretreatment methods of lignocellulosic material in order to use it as an efficient raw material for biofuel production will be discussed.

Source: Edited by Alejandro Rodríguez Pascual and María E. Eugenio Martín. “Microbial Cellulases: An Overview and Applications” Cellulose (2018)

Amylase

Amylase

INTRODUCTION Amylase is a digestive enzyme predominantly secreted by the pancreas and salivary glands and found in other tissues in very small levels. Amylase was first described in the early 1800s and is considered one of the first enzymes in history to be scientifically investigated. It was initially termed as diastase but was later renamed amylase in the early 20th century.
Amylases' main function is to hydrolyze the glycosidic bonds in starch molecules, converting complex carbohydrates to simple sugars. There are three main classes of amylase enzymes; Alpha-, beta- and gamma-amylase, and each act on different parts of the carbohydrate molecule. Alpha-amylase can be found in humans, animals, plants, and microbes. Beta-amylase is found in microbes and plants. Gamma-amylase is found in animals and plants. This article will focus on alpha-amylase and its applications.
In 1908, a study by Wohlgemuth identified the presence of amylase in urine, and this subsequently led to the use of amylase as a diagnostic laboratory test. Amylase is a commonly ordered test along with lipase, especially in the setting of suspected acute pancreatitis.

Source: Ololade Akinfemiwa and Thiruvengadam Muniraj. “Amylase” StatPearls (2022).

Protease

Proteases

Abstract

The processes of growth and remodeling of cells and tissues in multicellular organisms require the breakdown of old protein molecules, in concert with the synthesis of new ones. For example, many newly-synthesized molecules require proteolytic processing to convert them to biologically active forms. Proteolysis can terminate the activity of a protein--e.g., caspases mediate apoptosis, which is a vital step in the life cycle of the cell. Proteolysis contributes to defense systems too, as the recognition of peptide fragments of foreign proteins triggers the immune response. Proteases are the class of enzymes involved in these important reactions. This unit discusses the general categories of proteases, and sets the stage for addition of overview units on cysteine proteases, aspartic proteases, and metalloproteases, as well as protocol units featuring techniques for analyzing mammalian and yeast proteasomes and protease inhibitors, among other topics.

Source: A. J. Barrett. “Proteases” Current Protocols in Protein Science (2001): Chapter 21: Unit 21.1

Glycine

Glycine metabolism in animals and humans: implications for nutrition and health

Abstract

Glycine is a major amino acid in mammals and other animals. It is synthesized from serine, threonine, choline, and hydroxyproline via inter-organ metabolism involving primarily the liver and kidneys. Under normal feeding conditions, glycine is not adequately synthesized in birds or in other animals, particularly in a diseased state. Glycine degradation occurs through three pathways: the glycine cleavage system (GCS), serine hydroxymethyltransferase, and conversion to glyoxylate by peroxisomal D-amino acid oxidase. Among these pathways, GCS is the major enzyme to initiate glycine degradation to form ammonia and CO2 in animals. In addition, glycine is utilized for the biosynthesis of glutathione, heme, creatine, nucleic acids, and uric acid. Furthermore, glycine is a significant component of bile acids secreted into the lumen of the small intestine that is necessary for the digestion of dietary fat and the absorption of long-chain fatty acids. Glycine plays an important role in metabolic regulation, anti-oxidative reactions, and neurological function. Thus, this nutrient has been used to: (1) prevent tissue injury; (2) enhance anti-oxidative capacity; (3) promote protein synthesis and wound healing; (4) improve immunity; and (5) treat metabolic disorders in obesity, diabetes, cardiovascular disease, ischemia-reperfusion injuries, cancers, and various inflammatory diseases. These multiple beneficial effects of glycine, coupled with its insufficient de novo synthesis, support the notion that it is a conditionally essential and also a functional amino acid for mammals (including pigs and humans).

Source: Weiwei Wang, Zhenlong Wu, Zhaolai Dai, Ying Yang, Junjun Wang, and Guoyao Wu. “Glycine metabolism in animals and humans: implications for nutrition and health” Amino Acids (2013): 45(3):463-77.