Safety evaluation of enzyme detergents. Oral and cutaneous toxicity, irritancy and skin sensitization studies

Griffith, John F.; Weaver, James E.; Whitehouse, H. S.; Poole, Rob; Newmann, E.A.; Nixon, G.A.

doi:10.1016/s0015-6264(69)80461-x

Cited by 39 publications

(14 citation statements)

References 11 publications

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“…Enzyme proteins are not able to behave as classic haptens of the type associated with cell-mediated delayed hypersensitivity (reviewed in Divkovic et al, 2005). Thus they cannot function as skin sensitisers, an outcome which is fully consistent with the observation that enzymes do not produce this type of adverse effect in humans (Griffith et al, 1969;White et al, 1985;Basketter et al, 2008).…”

Section: Skinmentioning

confidence: 55%

“…However, a somewhat higher derived no-effect level (DNEL), 0.2%, expressed as% active enzyme protein, is regarded as safe under normal work exposure conditions, where the contact with skin is normally confined to a fraction of the hands (palms and/or fingers, skin areas where the epidermal thickness is greatest) and of very short duration (typically a few minutes at most). This conclusion is based on the existing dermal safety studies, including human studies (HERA, 2007;Griffith et al, 1969;Bolam et al, 1971). The NOEC of HERA was based on several dermal human safety studies, performed under worst case conditions (occlusion, typical 24 h of exposure, repeated dosing and/or scarified skin).…”

Section: Skinmentioning

confidence: 99%

See 1 more Smart Citation

Enzymes in cleaning products: An overview of toxicological properties and risk assessment/management

Basketter

Berg

Broekhuizen³

et al. 2012

Regulatory Toxicology and Pharmacology

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Section: Skinmentioning

confidence: 55%

Section: Skinmentioning

confidence: 99%

Enzymes in cleaning products: An overview of toxicological properties and risk assessment/management

Basketter

Berg

Broekhuizen³

et al. 2012

Regulatory Toxicology and Pharmacology

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“…Enzymes are used in a variety of industrial processes to create an array of foods (Foegeding and Larick, 1986;Cronlund and Woychik, 1987;Christensen, 1989;Ashie and Lanier, 2000;Dĩaz-López and García-Carreńo, 2000;Shahidi and JanakKamil, 2001), cosmetics (Griffith et al, 1969;Lods et al, 2000;Sim et al, 2000;Spök, 2006;Mohorcic et al, 2006), nutraceutical (Zhao, 2007;Zarevúcka and Wimmer, 2008;Guerard et al, 2010) and medicinal products (Agren et al, 1992;Takahashi et al, 1999;Mirastschijski et al, 2002;Püllen et al, 2002;Chung et al, 2004). Enzymatic methods offer advantages over chemical techniques such as substrate specificity and elevated activity under mild conditions that allow better control of the production processes (Zaks et al, 1988;Shahidi and JanakKamil, 2001).…”

Section: Introductionmentioning

confidence: 99%

Extraction and Purification of Collagenase Enzymes: A Critical Review

Daboor¹,

Budge²,

Ghaly

et al. 2010

American Journal of Biochemistry and Biotechnology

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Problem statement: Enzymes have vital roles in several industrial processes (foods, cosmetics, nutraceuticals and pharmaceuticals) due to their highly selective nature and high activity at very low concentrations. Recent efforts to identify new sources of useful enzymes have been concentrated on the marine environment because of the potential to make use of processing wastes. About 35-50% of the mass of the fish caught is a waste that is disposed off at sea or in landfills. The extraction of enzymes from fish processing waste can reduce environment problems and improve the economics of the fish industry. Collagenases are a group of enzymes that can be extracted from fish waste. Approach: Comprehensive reviews of the literature on the extraction, purification, characterization and use of collagenases was carried out. Results: Collagenases have different molecular weights based on their types and sources. They have the ability to break down the peptide bonds in collagen at physiological pH. They are classified into two types: serine and metallocollagenase. Collagenolytic activities have been shown at a wide range of temperatures (20-40°C) and pH (6-8). Many activators can be used to achive collagenase activity including 4-Aminophenylmercuric Acetate (APMA), trypsin, potassium or sodium thiocyanate, iodoacetamide and potassium iodide. Dithiothreitol (DTT), mercaptoethanol, ethylendiaminetetracetic acid, ophenanthroline and cysteine inactivate the enzyme. Collagenases enzymes can be extracted with a variety of techniques using different buffering systems (tris-HCl, sodium bicarbonate, calcium chloride and cacodylate). All techniques involve the use of ammonium sulphate fractionation and centrifugation to precipitate the enzyme. Collagenases are normally purified using chromatographic techniques such as gel-filtration, ion-exchange and affinity column chromatography. Collagenase can be assayed with a number of methods, including: colorimetric absorbance, viscometry, radioactivity and fluorescence spectroscopy. Collagenases are partly responsible for toughness in red meats and are used as tenderizers in food industry, have application in the fur and hide tanning to ensure uniform dying of leather, used in medicine to treat burns and ulcers, eliminate scar tissues, transplantation of organs. Conclusion: Understanding of the nature of the enzymes and identifying the most suitable resources and the methods for their extraction and purification will have significant impact on the fish processing, food and medical industries.

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“…Although animals ex posed by topical and abraded skin application produced antibodies in volved in immediate hypersensitivity reactions these same animals failed to produce delayed hypersensitivity reactions. Thus, it is not surprasing that G r iffith et al [11] failed to detect sensitization in consumers, guinea pigs and rabbits exposed to B. subtilis enzymes by topical appli cation since these authors used skin-irritation, an indicator of delayed reactions as the sole criteria of detection. Furthermore, in the present study, during the period to which the guinea pigs were exposed by inhal ation route there was no overt evidence of asthma-like episodes.…”

Section: Discussionmentioning

confidence: 99%

“…G riffith ct al. [11] found that the B. subtilis enzymes were not effective in causing contact sensitivities in a large group of consumer population nor in guinea pigs and rabbits. In addition, the acute oral administration of detergents containing B. subtil is enzymes to rats displayed a low order of oral toxicity.…”

mentioning

confidence: 94%

The Effect of Laundry Detergent Containing <i>B. subtilis</i> Enzyme in Producing Sensitization Reactions in Guinea Pigs

Perelmutter¹,

Lavallee²,

Wiberg³

1972

Int Arch Allergy Immunol

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Guinea pigs exposed to laundry detergents containing B. subtilis enzymes (alcalase) under home use conditions, i.e. by inhalation, abraded skin or topical application and oral ingestion, produced sensitization reactions. The jejunum smooth muscles of these animals contracted in the presence of alcalase and the sera caused morphological changes of rat mast cells in the presence of alcalase. It was found that long periods (50–60 days) of chronic exposure was necessary to produce sensitization. The relevance of these results to sensitization of consumers to B. subtilis enzymes in laundry detergent is discussed.

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Safety evaluation of enzyme detergents. Oral and cutaneous toxicity, irritancy and skin sensitization studies

Cited by 39 publications

References 11 publications

Enzymes in cleaning products: An overview of toxicological properties and risk assessment/management

Enzymes in cleaning products: An overview of toxicological properties and risk assessment/management

Extraction and Purification of Collagenase Enzymes: A Critical Review

The Effect of Laundry Detergent Containing <i>B. subtilis</i> Enzyme in Producing Sensitization Reactions in Guinea Pigs

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