Secondary structures of rat lipolytic enzymes: Circular dichroism studies and relation to hydrophobic moments

Jacobson, P W; Cornette, James L.

doi:10.1016/0006-291x(89)91967-0

Cited by 6 publications

(2 citation statements)

References 16 publications

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“…The percentage of β-turns/other secondary structure did not change significantly and remained 23.03 and 22.01%, respectively, but some unordered components of 10.81% at 1645 cm –1 were observed in nanoparticles. Other reports on the percentage of α helix of lipases from Rhizopus niveus (homologous to Rhizopus oryzae), Rhizomucor meihei and pancreatic lipase revealed the high percentage of α helix (>33%) in aqueous solution, − which is very close to the percentage of α-helix in nanoparticles we found in this study. These findings agree with previous reports that co-lyophilization of proteins with MβCD reduces structural changes occurring during lyophilization. , …”

Section: Resultssupporting

confidence: 89%

Synthesis of Rhizopus arrhizus Lipase Nanoparticles for Biodiesel Production

et al. 2018

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We developed a nanoparticulate Rhizopus arrhizus lipase formulation to enhance its activity and to increase the conversion yield of lipids into fatty acid methyl esters (FAME, a.k.a., biodiesel). More than 95% purity of the lipase was achieved in a two-step purification. Nanoparticle formulation was afforded by co-lyophilization of the lipase with methyl-βcyclodextrin (MβCD), an established lyoprotectant. Scanning electron microscopy and dynamic light scattering measurements showed a size of 75− 200 nm for the nanoparticles depending on the ratio of lipase-to-MβCD employed during co-lyophilization. Fourier transform infrared spectroscopic analysis by Gaussian curve fitting of the resolution-enhanced amide I region of lyophilized and nanoparticulate lipase indicated a more native-like secondary structure in the latter. A 98% substrate-to-FAME conversion was achieved in 10 h in n-hexane by lipase nanoparticles, whereas the crude and lyophilized enzyme showed 65 and 70% conversion in 18 h, respectively. In this aspect, the lipase nanoparticles were superior to all other reported systems. Operational stability after 5 catalytic conversions of nanoparticles was found to be >81%. In summary, we herein developed a novel lipase formulation for efficient catalysis in lipid-to-biodiesel conversion.

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Section: Resultssupporting

confidence: 89%

Synthesis of Rhizopus arrhizus Lipase Nanoparticles for Biodiesel Production

et al. 2018

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“…Both groups determined its amino acid composition; it appears to have an average hydrophobicity. The secondary structures of rat lingual lipase and pancreatic lipase were studied and compared by Roberts et al (1989). The gene for rat lingual lipase has been cloned and sequenced, and the amino acid sequence of the enzyme deduced (Docherty et al 1985).…”

Section: Lipases In Cheese Productionmentioning

confidence: 99%

Exogenous Enzymes in Dairy Technology ? A Review

Fox¹

1993

J Food Biochemistry

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A substantial number of enzymes have potential applications in dairy technology but most are not commercially viable, at least at present. In this review, the principal applications of proteinases (rennets for cheese manufacture, acceleration of cheese ripening, modification of the functional properties of milk proteins, preparation of nutritionally and physiologically active peptides), lipases (mainly in cheese ripening) and lysozyme are discussed.

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Table 7.IV

Yang¹,

Wu²,

Böhm³

Landolt-Börnstein - Group VII Biophysics

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Secondary structures of rat lipolytic enzymes: Circular dichroism studies and relation to hydrophobic moments

Cited by 6 publications

References 16 publications

Synthesis of Rhizopus arrhizus Lipase Nanoparticles for Biodiesel Production

Synthesis of Rhizopus arrhizus Lipase Nanoparticles for Biodiesel Production

Exogenous Enzymes in Dairy Technology ? A Review

Table 7.IV

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