Aim: An investigation was carried out on the production of a-amylase by Bacillus thermooleovorans NP54, its partial puri®cation and characterization. Methods and Results: The thermophilic bacterium was grown in shake¯asks and a laboratory fermenter containing 2% soluble starch, 0Á3% tryptone, 0Á3% yeast extract and 0Á1% K 2 HPO 4 at 70 C and pH 7Á0, agitated at 200 rev min À1 with 6-h-old inoculum (2% v/v) for 12 h. When the enzyme was partially puri®ed using acetone (80% [v/v] saturation), a 43Á7% recovery of enzyme with 6Á2-fold puri®cation was recorded. The K M and V max (soluble starch) values were 0Á83 mg ml À1 and 250 mmol mg À1 protein min À1 , respectively. The enzyme was optimally active at 100 C and pH 8Á0 with a half-life of 3 h at 100 C. Both a-amylase activity and production were Ca 2 independent. Conclusions: Bacillus thermooleovorans NP54 produced calcium-independent and thermostable a-amylase. Signi®cance and Impact of the Study: The calcium-independent and thermostable aamylase of B. thermooleovorans NP54 will be extremely useful in starch sacchari®cation since the a-amylases used in the starch industry are calcium dependent. The use of this enzyme in starch hydrolysis eliminates the use of calcium in starch liquefaction and subsequent removal by ion exchange.

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Biochemical Society Transactions ( 1 995) 23 539s d c o b Q I * b p b m OIL C m b Y oi13ood I mBlood is a tissue that circulates in what is virtually a closed system of blood vessels and consist of red and white cells and the platelets suspended in plasma. The specific cellular function of blood is to transport oxygen via hemoglobin. It has long been established that there is a relationship between drug or any other foreign substance administered in the blood and the pharmacological and toxic response caused thereby. The red blood cells contain heme whidh is Fe-PP (Iron-Protoporphyrin), therefore,the administration of its analogues like CoPP, CoMP, CoHP cause significant changes in the blood chemistry i.e. in lipid contents , liver and renal function [l].hrs. but were provided free access to water. After 24 hrs. animals were divided into five groups. Group I : Animals in this group were taken as control. Group I1 : Animals in this group were administered Cobaltprotoporphyrin (CoPP) (50 pM/kg b.w. s.c.). Group 111: Animals in this group were administeredGroup IV : Animals in this group were administered Cobalthematoporphyrin (CoHP) (50 p M / kg b.w. s.c.). After 24 hrs. blood was drawn from the heart of animals of all groups under sterile conditions. The blood was allowed to clot and serum was separated for the analysis of enzymes SGOT, SGPT, Alkaline phosphatase and other constituents of serum : Uric acid, Bilirubin, Cholesterol and Triglycerides.Aminotransferases catalyses the transfer of an amino group between L-alanine and L-Glutamate in case of GPT and between L-aspartate and L-glutamate in case of W T . Alkaline Phosphatase is an enzyme which hydrolyses a variety of organic phosphate esters. These enzymes are used in diagonsis of liver disease and are in the category of non-plasma specific enzymes i.e. concerned with intracellular metabolism and have no known function in plasma. They are released from the liver when parenchymal cells become nacrotic and the increase in their activity in the plasma is related to extent of cell breakdown. The rationale for assaying these enzymes in the liver is because of high levels of these enzymes present in this tissue. The assay of SGPT and S W T was carried out by the method of Young et.al [ 2 ] and Alkaline Phosphatase by the method of Amador et.al. [ 31. We have observed that both CoPP and CoMP lead to the induction of S W T by -2 and -1.2 fold respectively, while only CoPP leads to induction of SGPT by -1.15 fold and CoMP leads to decrease of level by -0.8 fold. CoHP didnot show any change in the level of either of these enzymes. Alkaline phosphatase also shows alteration by CoPP and CoHP -2 fold induction; whereas CoMP failed to evoke any response. Hyperuricemia is comnonly caused by abnormally rapid turnover of nucleic acid and due to relative insolubility of uric acid. The accumulation of uric acid above normal levels results in precipitation and formation of sodium urate crystals in kidney. The uric acid was estimated by the method of Young et.al. [ 2 ] . It was o...

Heme is a tetrapyrrolic ring with iron as the central metal atom and acts as a prosthetic group for a number of enzymes, e.g. cytochromes and globins. It also plays an important role in the regulation of transcription, translation, protein translocation and erythroid differentiation. Thus, heme regulation is under strict control in the body. Our studies on the regulatory enzymes of heme anabolism, aminolevulinic acid synthetase (ALA-S), and of catabolism, heme oxygenase (HMOX), in the spleen has revealed that cobalt protoporphyrin acts as an inducer of HMOX. It is revealed that by alteration of side groups at C2 and C4 changes the nature of action of Co-protoporphyrin from an inducer to a strong inhibitor of HMOX activity. All the three analogues Co-protoporphyrin, Co-mesoporphyrin and Co-hematoporphyrin have been shown to induce the ALA-S activity to the similar extent. NADPH-cytochrome c reductase, a microsomal membrane bound enzyme, is required by HMOX for the enzymatic conversion of heme into biliverdin IXc and is also required for NADPH-dependent lipid peroxidation in the microsomes. It has been observed that Co-mesoporphyrin causes an inhibition of HMOX activity and consequently leads to an induced level of microsomal NADPH-dependent lipid peroxidation.