Enzyme amylases

Enzymes act as catalysts to increase the rates of chemical reactions, but they do not cause a reaction to occur that would not proceed spontaneously without the enzyme. Digestive enzymes help break down foods so their nutrients can be absorbed effectively through the gut and utilized by the body, such as for energy and to build and repair the body. During the sprouting process, enzymes are increased, helping to make seeds, nuts, legumes and grains much easier to digest.

Human saliva and pancreatic secretion contain a large amount of α-amylase for starch digestion. The specificity of the bond attacked by alpha-amylases depends on the sources of the enzymes. Salivary amylase initiates carbohydrate digestion in the mouth and pancreatic amylase is the main enzyme for luminal digestion of carbohydrate in the small intestine.

α-amylase (1,4-α-D-glucan-glucanohydrolase,) is the primary digestive enzyme acting on starch or glycogen and is present in plants, animals, bacteria and fungi.

Starch degrading amylolytic enzymes are most important in the biotechnology industries. Their uses range from textiles, beer, liquor, bakery, infant feeding cereals, starch liquefaction-saccharification, animal feed industries to chemical and pharmaceutical uses.

Amylases can be obtained from several sources such as plant, animal, and microbes. The microbial source of amylase is preferred to other sources because of its plasticity and vast availability. The species Aspergillus and Rhizopus are highly important among the filamentous fungus for the production of amylases.
Enzyme amylases

Lipase enzyme

Lipases (triacylglycerol ester hydrolase) are enzymes that catalyze the total or partial hydrolysis of fats and oils, releasing free fatty acids, diacylglycerols, monoacylglycerols and glycerol. Lipases occur widely in nature, but only microbial lipases are commercially significant.

Lipase was first discovered in pancreatic juice as an enzyme by Claude Bernard in 1856, which hydrolyzed unsolvable oil droplets and transformed them to soluble products. After that the productions of lipase have been observed in the bacteria Bacillus prodigiosus, B. pyocyaneus and B. fluorescens in 1901.

A true lipase will split emulsified esters of glycerine and long-chain fatty acids such as triolein and tripalmitin. Lipases, in thermodynamic favorable conditions (i.e., low water activity), catalyze a large variety of synthesis reactions which can be classified into two main types of reactions, i.e.,
*Esterification
*Transesterification

They do not require any cofactor and belongs to the class of serine hydrolases. Triglycerides hydrolyzed into diglycerides, monoglycerides, fatty acids, and glycerol by using the lipases naturally.

Esterification is the reaction where a fatty acid is linked, through the action of the enzyme, to an alcohol by a covalent bond, producing an ester and releasing a water molecule. Thioesterification and amidation are similar reactions but with a thiol or an amine as substrates.

Transesterification groups alcoholysis, acidolysis, aminolysis, and interesterification reactions.

The molecular weight of lipases is in the range of 19–60 kDa and reported to be monomeric protein. The position of the fatty acid in the glycerol backbone, chain length of the fatty acid, and its degree of unsaturation are the factors and the physical properties of lipases depend on it.

The many applications of lipases include speciality organic syntheses, hydrolysis of fats and oils, modification of fats, flavor enhancement in food processing, resolution of racemic mixtures, and chemical analyses.

In the food industry, lipases can be used as flavor modifiers by synthesis of short chain fatty acids esters and alcohols, and to obtain products of increased nutritional value by modifying the triacylglycerol structure for inter- or transesterification. In bakery, lipases are potential candidate substitutes for emulsifiers.

Microbial lipases are produced mostly by submerged culture, but solid-state fermentation methods. Lipase production is influenced by the type and concentration of carbon and nitrogen sources, the culture pH, the growth temperature, and the dissolved oxygen concentration.
Lipase enzyme

Vitaminlike substance of coenzyme Q10

Coenzyme Q10 is a vitamin substance found in all parts of the body the action of which resembles that of vitamin E. It is also called ubiquinone, is one form o a substance known coenzyme Q that is found in all plant and animal cells.

It may be an even more powerful antioxidant. Coenzyme Q10 protects human body against free radicals the destructive molecular fragment that cause accelerated aging and degenerative disease.

There are ten common substances designated coenzyme Qs, but coenzyme Q10 is the only one found in human tissue.

It is a fundamental ingredient in the energy production that keeps those trillion of cells running smoothly. Coenzyme Q10 is especially well-known for its ability to prevent cellular damage during and following a heart attack – myocardial ischemia and reperfusion.

It aids circulation, stimulates the immune system, increases tissue oxygenation, and has vital anti-aging effects.

Deficiencies of coenzymes Q10 have been linked to periodontal disease, diabetes and muscular dystrophy. Coenzyme Q10 can help reduce muscle damage from oxidation during strenuous exercise and reduce muscle soreness.

Supplemental has ability to counter histamine and therefore beneficial for people with allergies, asthma or respiratory disease.

Coenzyme Q10 is used by many health care professional. To treat anomalies of mental function, such as those associated with schizophrenia and Alzheimer’s disease.

It is also benefiting in fighting obesity, candidiasis, multiple sclerosis and diabetes.

Coenzyme Q10 is widely distributed in foods, but only in small amounts. Soybeans, walnuts, and almonds, meats, certain fish, nuts, wheat germ, and some vegetables, are the best sources.
Vitaminlike substance of coenzyme Q10