Safety Evaluation of Lipase Produced from Candida rugosa: Summary of Toxicological Data

Flood, Michael T.; Kondo, Mitsuru

doi:10.1006/rtph.2001.1464

Cited by 14 publications

(9 citation statements)

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“…Candida rugosa was found to possess no genotoxic potential when subjected to a battery of tests including bacterial mutation in Salmonella typhimurium strains TA98, TA100, TA1535, and TA1537 and in E. coli strain WP2 uvrA, in vitro chromosome aberration, and forward mutation in L5178Y mouse lymphoma cells (61). The yeast producing CRL was nonpathogenic to mice at doses up to 1.5 × 10 7 CFU/body.…”

Section: Regulatory and Safety Considerationsmentioning

confidence: 99%

Protein engineering and applications of Candida rugosa lipase isoforms

Akoh

Lee

Shaw

2004

Lipids

102

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Commercial preparations of Candida rugosa lipase (CRL) are mixtures of lipase isoforms used for the hydrolysis and synthesis of various esters. The presence of variable isoforms and the amount of lipolytic protein in the crude lipase preparations lead to a lack of reproducibility of biocatalytic reactions. Purification of crude CRL improve their substrate specificity, enantioselectivity, stability, and specific activities. The expression of the isoforms is governed by culture or fermentation conditions. Unfortunately, the nonsporogenic yeast C. rugosa does not utilize the universal codon CTG for leucine; therefore, most of the CTG codons were converted to universal serine triplets by site-directed mutagenesis to gain expression of functional lipase in heterologous hosts. Recombinant expressions by multiple-site mutagenesis or complete synthesis of the lipase gene are other possible ways of obtaining pure and different CRL isoforms, in addition to culture engineering. Protein engineering of purified CRL isoforms allows the tailoring of enzyme function. This involves computer modeling based on available 3-D structures of lipase isoforms. Lid swapping and DNA shuffling techniques can be used to improve the enantioselectivity, thermostability, and substrate specificity of CRL isoforms and increase their biotechnological applications. Lid swapping can result in chimera proteins with new functions. The sequence of the lid can affect the activity and specificity of recombinant CRL isoforms. Candida rugosa lipase is toxicologically safe for food applications. Protein engineering through lid swapping and rationally designed site-directed mutagenesis will continue to lead to the production of CRL isoforms with improved catalytic power, thermostability, enantioselectivity, and substrate specificity, while providing evidence for the mechanisms of actions of the various isoforms.

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Section: Regulatory and Safety Considerationsmentioning

confidence: 99%

Protein engineering and applications of Candida rugosa lipase isoforms

Akoh

Lee

Shaw

2004

Lipids

102

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“…Enzyme preparations from CRL are considered safe to workers and consumers and they can be used in industrial applications . That is why diverse products (ranging from dairy enrichment, desirable flavors as additive in food, and the interesterification of fats and oils to pharmaceuticals and biodiesel) are already manufactured by free or immobilized Candida rugosa lipases.…”

Section: Current and Promising (Industrial) Applicationsmentioning

confidence: 99%

“…Enzyme preparations from CRL are considered safe to workers and consumers and they can be used in industrial applications. 100 That is why diverse products (ranging from dairy enrichment, desirable flavors as additive in food, and the interesterification of fats and oils to pharmaceuticals and biodiesel) are already manufactured by free or immobilized Candida rugosa lipases. Another key reason why lipases are already used in the industry is their ability to perform very specific chemical transformations such as enantioselective reactions, which cannot be performed by nonbiocatalysts.…”

Section: ■ Substrate Specificitymentioning

confidence: 99%

Substrate-Specificity ofCandida rugosaLipase and Its Industrial Application

Vanleeuw

Winderickx

Thevissen

et al. 2019

ACS Sustainable Chem. Eng.

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Candida rugosa lipase (CRL) is a very versatile and widely used lipase in the aroma and flavor industry, the fat and oil industry, the pharmaceutical industry and is also applicable as a biosensor. The present paper discusses recent developments on the molecular level of CRL, the biocatalytic reactivity of several Lip isoenzymes, diverse immobilization strategies of the enzyme and its broad (substrate) specificities in different fields. Furthermore, an overview is given of future applications with CRL such as the enantioselective hydrolysis of racemic lactate esters produced out of sugars and the production of biodiesel out of vegetable oil. These processes have been tried on laboratory scale but still need further optimization for industrialization.

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“…Another phenomenon was observed that the mice began to struggle when the dose increased to 1535 mg/kg, while no struggling was observed on mice for the seven-day repeated toxicity, suggesting that this adverse effect was dose dependent. Commonly, abnormal alterations to body weight in toxicity studies have been regarded as critical indicators of adverse effects [ 19 ]. No significant alteration to body weight was found, both in the acute and repeated dose study at all doses, implying that SalB-Rg1 was well tolerated by the mice.…”

Section: Discussionmentioning

confidence: 99%

The Safety Evaluation of Salvianolic Acid B and Ginsenoside Rg1 Combination on Mice

Zhao

Yang

Deng

et al. 2015

IJMS

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Our previous study indicated that the combination of salvianolic acid B (SalB) and ginsenoside Rg1 (Rg1), the main components of Salvia miltiorrhizae and Panax notoginseng, improves myocardium structure and ventricular function in rats with ischemia/reperfusion injury. The present study aimed to determine the safety of the combined SalB and Rg1 (SalB-Rg1) in mice. The safety of SalB-Rg1 was evaluated through acute toxicity and repeated-dose toxicity. In the acute toxicity study, the up and down procedure was carried out firstly, and then, the Bliss method was applied. In the toxicity study for seven-day repeated treatment of SalB-Rg1, forty Kunming mice were randomly divided into four groups. The intravenous median lethal dose (LD50) of the SalB-Rg1 combination was 1747 mg/kg using the Bliss method. For both the acute toxicity study and the seven-day repeated toxicity study, SalB-Rg1 did not induce significant abnormality on brain, heart, kidney, liver and lung structure at any dose based on H&E stain. There were no significant changes related to the SalB-Rg1 toxicity detected on biochemical parameters for two kinds of toxicity studies. The LD50 in mice was 1747 mg/kg, which was more than one hundred times higher than the effective dose. Both studies of acute toxicity and seven-day repeated dose toxicity indicated the safety of the SalB-Rg1 combination.

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Safety Evaluation of Lipase Produced from Candida rugosa: Summary of Toxicological Data

Cited by 14 publications

References 0 publications

Protein engineering and applications of Candida rugosa lipase isoforms

Protein engineering and applications of Candida rugosa lipase isoforms

Substrate-Specificity ofCandida rugosaLipase and Its Industrial Application

The Safety Evaluation of Salvianolic Acid B and Ginsenoside Rg1 Combination on Mice

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