148 BIOLOGY etc. (Table 9.5). Collagen is the most abundant protein in animal world and Ribulose bisphosphate Carboxylase-Oxygenase (RuBisCO) is the most abundant protein in the whole of the biosphere. 9.5 POLYSACCHARIDES The acid insoluble pellet also has polysaccharides (carbohydrates) as another class of macromolecules. Polysaccharides are long chains of sugars. They are threads (literally a cotton thread) containing different monosaccharides as building blocks. For example, cellulose is a polymeric polysaccharide consisting of only one type of monosaccharide i.e., glucose. Cellulose is a homopolymer. Starch is a variant of this but present as a store house of energy in plant tissues. Animals have another variant called glycogen. Inulin is a polymer of fructose. In a polysaccharide chain (say glycogen), the right end is called the reducing end and the left end is called the non-reducing end. It has branches as shown in the form of a cartoon (Figure 9.2). Starch forms helical secondary structures. In fact, starch can hold I2 molecules in the helical portion. The starch-I2 is blue in colour. Cellulose does not contain complex helices and hence cannot hold I2. O O O O O CH OH2 OH OH O O CH OH2 OH OH OH O O CH2 O O O O Figure 9.2 Diagrammatic representation of a portion of glycogen BIOLOGY 9.12 ENZYMES Almost all enzymes are proteins. There are some nucleic acids that behave like enzymes. These are called ribozymes. One can depict an enzyme by a line diagram. An enzyme like any protein has a primary structure, i.e., amino acid sequence of the protein. An enzyme like any protein has the secondary and the tertiary structure. When you look at a tertiary structure (Figure 9.4 b) you will notice that the backbone of the protein chain folds upon itself, the chain criss-crosses itself and hence, many crevices or pockets are made. One such pocket is the ‘active site’. An active site of an enzyme is a crevice or pocket into which the substrate fits. Thus enzymes, through their active site, catalyse reactions at a high rate. Enzyme catalysts differ from inorganic catalysts in many ways, but one major difference needs mention. Inorganic catalysts work efficiently at high temperatures and high pressures, while enzymes get damaged at high temperatures (say above 40°C). However, enzymes isolated from organisms who normally live under extremely high temperatures (e.g., hot vents and sulphur springs), are stable and retain their catalytic power even at high temperatures (upto 80°-90°C). Thermal stability is thus an important quality of such enzymes isolated from thermophilic organisms. 9.12.1 Chemical Reactions How do we understand these enzymes? Let us first understand a chemical reaction. Chemical compounds undergo two types of changes. A physical change simply refers to a change in shape without breaking of bonds. This is a physical process. Another physical process is a change in state of matter: when ice melts into water, or when water becomes a vapour. These are also physical processes. However, when bonds are broken and new bonds are formed during transformation, this will be called a chemical reaction. For example: Ba(OH) + HSO→ BaSO + 2HO224 42is an inorganic chemical reaction. Similarly, hydrolysis of starch into glucose is an organic chemical reaction. Rate of a physical or chemical process refers to the amount of product formed per unit time. It can be expressed as: δ P rate = δ t Rate can also be called velocity if the direction is specified. Rates of physical and chemical processes are influenced by temperature among other factors. A general rule of thumb is that rate doubles or decreases by half BIOMOLECULES for every 10°C change in either direction. Catalysed reactions proceed at rates vastly higher than that of uncatalysed ones. When enzyme catalysed reactions are observed, the rate would be vastly higher than the same but uncatalysed reaction. For example Carbonic anhydraseCO + HO ⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯→ HCO2223←⎯⎯⎯ carbon dioxide water carbonic acid In the absence of any enzyme this reaction is very slow, with about 200 molecules of H2CO3 being formed in an hour. However, by using the enzyme present within the cytoplasm called carbonic anhydrase, the reaction speeds dramatically with about 600,000 molecules being formed every second. The enzyme has accelerated the reaction rate by about 10 million times. The power of enzymes is incredible indeed! There are thousands of types of enzymes each catalysing a unique chemical or metabolic reaction. A multistep chemical reaction, when each of the steps is catalysed by the same enzyme complex or different enzymes, is called a metabolic pathway. For example, Glucose → 2 Pyruvic acid CHO + O → 2CH O + 2HO 61262 343 2 is actually a metabolic pathway in which glucose becomes pyruvic acid through ten different enzyme catalysed metabolic reactions. When you study respiration in Chapter 14 you will study these reactions. At this stage you should know that this very metabolic pathway with one or two additional reactions gives rise to a variety of metabolic end products. In our skeletal muscle, under anaerobic conditions, lactic acid is formed. Under normal aerobic conditions, pyruvic acid is formed. In yeast, during fermentation, the same pathway leads to the production of ethanol (alcohol). Hence, in different conditions different products are possible. 9.12.2 How do Enzymes bring about such High Rates of Chemical Conversions? To understand this we should study enzymes a little more. We have already understood the idea of an ‘active site’. The chemical or metabolic conversion refers to a reaction. The chemical which is converted into a product is called a ‘substrate’. Hence enzymes, i.e. proteins with three dimensional structures including an ‘active site’, convert a substrate (S) into a product (P). Symbolically, this can be depicted as: S → P It is now understood that the substrate ‘S’ has to bind the enzyme at its ‘active site’ within a given cleft or pocket. The substrate has to diffuse BIOLOGY biomolecules. Amino acids, monosaccharide and disaccharide sugars, fatty acids, glycerol, nucleotides, nucleosides and nitrogen bases are some of the organic compounds seen in living organisms. There are 20 types of amino acids and 5 to glycerol. Phospholipids contain, in addition, a phosphorylated nitrogenous compound. Only three types of macromolecules, i.e., proteins, nucleic acids and polysaccharides are found in living systems. Lipids, because of their association with membranes separate in the macromolecular fraction. Biomacromolecules are polymers. They are made of building blocks which are different. Proteins are heteropolymers made of amino acids. Nucleic acids (RNA and DNA) are composed of nucleotides. Biomacromolecules have a hierarchy of structures – primary, secondary, tertiary and quaternary. Nucleic acids serve as genetic material. Polysaccharides are components of cell wall in plants, fungi and also of the exoskeleton of arthropods. They also are storage forms of energy (e.g., starch and glycogen). Proteins serve a variety of cellular functions. Many of them are enzymes, some are antibodies, some are receptors, some are hormones and some others are structural proteins. Collagen is the most abundant protein in animal world and Ribulose bisphosphate Carboxylase-Oxygenase (RuBisCO) is the most abundant protein in the whole of the biosphere. Enzymes are proteins which catalyse biochemical reactions in the cells. Ribozymes are nucleic acids with catalytic power. Proteinaceous enzymes exhibit substrate specificity, require optimum temperature and pH for maximal activity. They are denatured at high temperatures. Enzymes lower activation energy of reactions and enhance greatly the rate of the reactions. Nucleic acids carry hereditary information and are passed on from parental generation to progeny. EXERCISES 1. What are macromolecules? Give examples. 2. Illustrate a glycosidic, peptide and a phospho-diester bond. 3. What is meant by tertiary structure of proteins? 4. Find and write down structures of 10 interesting small molecular weight biomolecules. Find if there is any industry which manufactures the compounds by isolation. Find out who are the buyers. 5. Proteins have primary structure. If you are given a method to know which amino acid is at either of the two termini (ends) of a protein, can you connect this information to purity or homogeneity of a protein? 6. Find out and make a list of proteins used as therapeutic agents. Find other applications of proteins (e.g., Cosmetics etc.) 7. Explain the composition of triglyceride. BIOMOLECULES 8. Can you describe what happens when milk is converted into curd or yoghurt, from your understanding of proteins. 9. Can you attempt building models of biomolecules using commercially available atomic models (Ball and Stick models). 10. Attempt titrating an amino acid against a weak base and discover the number of dissociating ( ionizable ) functional groups in the amino acid. 11. Draw the structure of the amino acid, alanine. 12. What are gums made of? Is Fevicol different? 13. Find out a qualitative test for proteins, fats and oils, amino acids and test any fruit juice, saliva, sweat and urine for them. 14. Find out how much cellulose is made by all the plants in the biosphere and compare it with how much of paper is manufactured by man and hence what is the consumption of plant material by man annually. What a loss of vegetation! 15. Describe the important properties of enzymes.