Lysosomal Triglyceride Lipase from the Lateral Line Tissue of Rainbow Trout (Salmo gairdneri)

1971 ◽  
Vol 28 (7) ◽  
pp. 1015-1018 ◽  
Author(s):  
E. Bilinski ◽  
R. E. E. Jonas ◽  
Y. C. Lau
Keyword(s):  
Rainbow Trout ◽  
Lateral Line ◽  
Lysosomal Enzymes ◽  
Lipolytic Activity ◽  
Mitochondrial Fraction ◽  
Maximum Activity ◽  
Salmo Gairdneri ◽  
Acid Lipase ◽  
Triton X ◽  
Hydrolysis Of

An acid lipase active toward tripalmitin and having the characteristics of lysosomal enzymes was shown to occur in the red lateral line tissue of rainbow trout (Salmo gairdneri). The enzyme showed maximum activity at pH 4–4.5. Triton X-100 (0.2–2.0%) strongly stimulated the activity of the acid lipase, but it inhibited markedly the lipolytic activity above pH 7. NaF (20 mM) and Na-p-chloromercuriphenyl-sulfonate (1 mM) partially inhibited the acid lipase. Fractionation of the total homogenate by differential centrifugation in 0.25 M sucrose showed that the acid lipase was present at highest concentration in the light mitochondrial fraction. Palmitic acid and dipalmitin were the two main products of hydrolysis of tripalmitin.

Lipolytic Activity Toward Long-Chain Triglycerides in Lateral Line Muscle of Rainbow Trout (Salmo gairdneri)

1969 ◽  
Vol 26 (7) ◽  
pp. 1857-1866 ◽  
Author(s):  
E. Bilinski ◽  
Y. C. Lau
Keyword(s):  
Rainbow Trout ◽  
Lateral Line ◽  
Lipolytic Activity ◽  
Salmo Gairdneri ◽  
Tissue Slices ◽  
Optimum Activity ◽  
Long Chain Triglycerides ◽  
Long Chain

Lipolytic activity toward long-chain triglycerides was studied in the lateral line muscle of rainbow trout (Salmo gairdneri) by use of tissue slices. Emulsification of substrates with phospholipids was found to be necessary to demonstrate lipolysis, which occurred in decreasing intensity with tripalmitin, triolein, and tristearin. The lipolytic activity showed optimum activity at pH 7.3 and it was inhibited by NaF, protamine, and p-chloromercuriphenyl sulfonate. Albumin had little effect on the activity. Epinephrine did not stimulate lipolysis, but it reduced loss of activity during preincubation.

scholarly journals Production of Thermophilic Chitinase by Paenibacillus sp. TKU052 by Bioprocessing of Chitinous Fishery Wastes and Its Application in N-acetyl-D-glucosamine Production

Polymers ◽  
2021 ◽  
Vol 13 (18) ◽  
pp. 3048
Author(s):  
Chien Thang Doan ◽  
Thi Ngoc Tran ◽  
San-Lang Wang
Keyword(s):  
Enzyme Production ◽  
Production Cost ◽  
Maximum Activity ◽  
Paenibacillus Sp ◽  
Negative Effect ◽  
Chitinase Production ◽  
Tween 40 ◽  
Triton X ◽  
Catalytic Functions ◽  
Hydrolysis Of

The bioprocessing of chitinous fishery wastes (CFWs) to chitinases through fermentation approaches has gained importance owing to its great benefits in reducing the enzyme production cost, and utilizing chitin waste. In this work, our study of the chitinase production of Paenibacillus sp. TKU052 in the presence of different kinds of CFWs revealed a preference for demineralized crab shells powder (deCSP); furthermore, a 72 kDa chitinase was isolated from the 0.5% deCSP-containing medium. The Paenibacillus sp. TKU052 chitinase displayed maximum activity at 70 °C and pH 4–5, while Zn2+, Fe3+, Triton X-100, Tween 40, and SDS exerted a negative effect on its activity, whereas Mn2+ and 2-mercaptoethanol were found to potentially enhance the activity. Among various kinds of polysaccharide, Paenibacillus sp. TKU052 chitinase exhibited the best catalytic activity on colloidal chitin (CC) with Km = 9.75 mg/mL and Vmax = 2.43 μmol/min. The assessment of the hydrolysis of CC and N-acetyl chitooligosaccharides revealed that Paenibacillus sp. TKU052 chitinase possesses multiple catalytic functions, including exochitinase, endochitinase, and N-acetyl-β-D-glucosaminidase activities. Finally, the combination of Paenibacillus sp. TKU052 chitinase and Streptomyces speibonae TKU048 N-acetyl-β-D-glucosaminidase could efficiently convert CC to N-acetyl-D-glucosamine (GlcNAc) with a production yield of 94.35–98.60% in 12–24 h.

Effects of Coenzyme A and Carnitine on Fatty Acid Oxidation by Rainbow Trout Mitochondria

1970 ◽  
Vol 27 (5) ◽  
pp. 857-864 ◽  
Author(s):  
E. Bilinski ◽  
R. E. E. Jonas
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Rainbow Trout ◽  
Fatty Acid Oxidation ◽  
Lateral Line ◽  
Coenzyme A ◽  
Maximal Activity ◽  
Salmo Gairdneri ◽  
Acid Oxidation ◽  
Mitochondrial Fractions

The effects of coenzyme A (CoA) and carnitine on the oxidation of 0.1 mM K-palmitate-1-14C and K-oleate-1-14C by mitochondrial fractions from lateral line muscle, white muscle, heart, liver, and kidney was studied in rainbow trout (Salmo gairdneri). CoA (0.01–0.10 mM) stimulated the oxidation of fatty acids by mitochondria from lateral line muscle and heart. With all the preparations of mitochondria, fatty acid oxidation was increased by addition of carnitine (1.0 mM) and in the presence of carnitine (1.0 mM), CoA (0.1–1.0 mM) gave a further increase in oxidative activity. Mitochondria from lateral line muscle and heart showed the same range of maximal activity (oxidized substrate at 15 C = 180–200 nmoles/mg N per hr), which was considerably above that found with mitochondria from other tissues. The results suggest similarities in the energy-supplying metabolism in lateral line muscle and heart of trout with respect to the utilization of fatty acids.

Lecithinase Activity in the Muscle of Rainbow Trout (Salmo gairdnerii)

1966 ◽  
Vol 23 (2) ◽  
pp. 207-220 ◽  
Author(s):  
E. Bilinski ◽  
R. E. E. Jonas
Keyword(s):  
Rainbow Trout ◽  
Lateral Line ◽  
White Muscle ◽  
Radioactive Tracer ◽  
Enzymic Activity ◽  
The Other ◽  
Level Of Activity ◽  
Hydrolysis Of ◽  
Trout Muscle

A radioactive tracer procedure for determination of the various lecithin hydrolysing enzymes, at a low level of activity, is described. The procedure involves the use of phospholipids labeled with C14in the choline moiety as substrate and the measurement of radioactivity released in the various products of hydrolysis. The pathway of lecithin catabolism in trout muscle is via glycerylphosphorylcholine. Of the other possible routes of breakdown of lecithin, there was no indication for the activity of phospholipase C or D. Greater enzymic activity was present in the lateral line muscle than in the white muscle. The enzyme which is responsible for hydrolysis of lecithin to glycerylphosphorylcholine showed optimum activity in the vicinity of pH 7 did not require Ca++for activity and was partially inhibited by Hg++. A lysolecithinase, showing similar properties, but having a comparatively greater activity, was also present in trout muscle.

Phosphatidylglycerophosphate synthase activity in Saccharomyces cerevisiae

1983 ◽  
Vol 29 (10) ◽  
pp. 1452-1457 ◽  
Author(s):  
George M. Carman ◽  
Charles J. Belunis
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mitochondrial Fraction ◽  
Maximum Activity ◽  
Energy Of Activation ◽  
Ph Optimum ◽  
Optimal Activity ◽  
Nonionic Detergent ◽  
Triton X

Cytidine 5′-diphospho-1,2-diacyl-sn-glycerol (CDP-diacylglycerol):sn-glycerol-3-phosphate phosphatidyltransferase (phosphatidylglycerophosphate synthase, EC 2.7.8.5) activity was characterized from the mitochondrial fraction of Saccharomyces cerevisiae. The pH optimum for the reaction was 7.0. Maximum activity was dependent on manganese (0.1 mM), magnesium (0.3 mM), or cobalt (1 mM) ions and the nonionic detergent Triton X-100 (1 mM). The apparent Km values for CDP-diacylglycerol and glycerol-3-phosphate were 33 and 27 μM, respectively. Optimal activity was at 30 °C with an energy of activation of 5.4 kcal/mol (1 cal = 4.1868 J). Phosphatidylglycerophosphate synthase activity was thermally labile above 40 °C. p-Chloromecuriphenylsulfonic acid, N-ethylmaleimide, and mercurous ions inhibited activity. Phosphatidylglycerophosphate synthase activity was partially solubilized from the mitochondrial fraction with 1% Triton X-100.

scholarly journals Intralysosomal hydrolysis of glycyl-l-phenylalanine 2-naphthylamide

1984 ◽  
Vol 219 (3) ◽  
pp. 965-970 ◽  
Author(s):  
M Jadot ◽  
C Colmant ◽  
S Wattiaux-De Coninck ◽  
R Wattiaux
Keyword(s):  
Membrane Permeability ◽  
High Activity ◽  
Incubation Medium ◽  
Total Activity ◽  
Mitochondrial Fraction ◽  
Cathepsin C ◽  
Permeability Studies ◽  
Triton X ◽  
Hydrolysis Of ◽  
Free Activity

Glycyl-L-phenylalanine 2-naphthylamide (Gly-L-Phe-2-NNap), a cathepsin C substrate, induces an increase of the free and unsedimentable activities of this enzyme when incubated with a total mitochondrial fraction of rat liver. 1 mM-ZnSO4 considerably inhibits the cathepsin C total activity, measured with Gly-L-Phe-2-NNap as the substrate, in the presence of Triton X-100. The inhibition is markedly less pronounced when the free activity is determined; a high activity remains that depends on the integrity of the lysosomes; it decreases as the free activity of N-acetylglucosaminidase increases when lysosomes are subjected to treatments able to disrupt their membrane. Cathepsin C activity is reduced when thioethylamine hydrochloride is omitted from the incubation medium. Under these conditions at 37 degrees C, the free activity equals the total activity, although the lysosomes are intact, as indicated by the low free activity of N-acetylglucosaminidase. 1 mM-ZnSO4 strikingly inhibits the total activity, whereas more than 80% of the free activity remains. These observations are presented as evidence that Gly-L-Phe-2-NNap can possibly cause a disruption of the lysosomes as a result of its hydrolysis inside these organelles. In the presence of ZnSO4, intralysosomal hydrolysis becomes apparent, owing to a preferential inhibition by Zn2+ of extralysosomal hydrolysis; in the absence of thioethylamine hydrochloride, it is measurable because the disruption of lysosomes by Gly-L-Phe-2-NNap is delayed as a result of a slow-down of the reaction. The usefulness of Gly-L-Phe-2-NNap and related dipeptidyl naphthylamides in lysosomal-membrane-permeability studies is emphasized.

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