Mechanistic studies of proteases and lipases for the detergent industry

Aaslyng, Dorrit; Gormsen, Erik; Malmos, Henrik

doi:10.1002/jctb.280500304

Cited by 51 publications

(33 citation statements)

References 1 publication

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“…Fungal lipases function in the removal of stains from fabrics and are important components of detergent mixtures [33]. As early as 1988, the company Novo Nordisk developed a fungal lipase, an enzyme capable of dissolving fatty stains.…”

Section: In Detergent Industrymentioning

confidence: 99%

Overview of Fungal Lipase: A Review

Singh

Mukhopadhyay

2011

Appl Biochem Biotechnol

351

200

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Lipases (triacylglycerolacyl hydrolases, EC3.1.1.3) are class of enzymes which catalyze the hydrolysis of long-chain triglycerides. In this review paper, an overview regarding the fungal lipase production, purification, and application is discussed. The review describes various industrial applications of lipase in pulp and paper, food, detergent, and textile industries. Some important lipase-producing fungal genera include Aspergillus, Penicillium, Rhizopus, Candida, etc. Current fermentation process techniques such as batch, fed-batch, and continuous mode of lipase production in submerged and solid-state fermentations are discussed in details. The purification of lipase by hydrophobic interaction chromatography is also discussed. The development of mathematical models applied to lipase production is discussed with special emphasis on lipase engineering.

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Section: In Detergent Industrymentioning

confidence: 99%

Overview of Fungal Lipase: A Review

Singh

Mukhopadhyay

2011

Appl Biochem Biotechnol

351

200

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“…Alkaline proteases are robust enzymes with considerable biotechnological potential for industrial sectors like detergents, processing of leather, recovery of silver, medical purposes, food processing, feeds and chemical industry, as well as in waste treatment [1][2][3]. The global proteolytic enzyme demand should reach to 22.0 billon dollars by 2009 [4].…”

Section: Introductionmentioning

confidence: 99%

Studies on Improving the Immobilized Bead Reusability and Alkaline Protease Production by Isolated Immobilized Bacillus circulans (MTCC 6811) Using Overall Evaluation Criteria

Rao

Madhavendra

Rao³

et al. 2008

Appl Biochem Biotechnol

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This study uses an overall evaluation criterion for improving the immobilized bead reusability and extracellular enzyme production by immobilized cells by assigning relative weightage to bead reusability, enzyme production, and cell leakage. Initially, alkaline protease production by alginate-immobilized Bacillus circulans (MTCC 6811) was analyzed using L18 orthogonal array (OA). The resultant optimized parameters were further fine-tuned with L9 OA experimentation. At L18-OA analysis, inoculum level and CaCl(2) had least influence at individual level. At the interactive level, incubation time revealed maximum and minimum interaction with sodium alginate and glucose concentration, respectively. L9 experimentation indicated that glucose concentration contributed the major influence on protease production followed by matrix material and incubation time at the individual level, and at the interactive level, matrix concentration played a vital role by interacting with incubation time, inoculum, and CaCl(2) concentration. All selected input parameters showed significance either at individual level or interactive in both OAs. Scanning electron microscopy analysis showed bacterial morphology variation with variation of matrix concentration. Overall, glucose concentration depicted a major influence at the individual level for the enzyme production. Significant improvement, approximately 147%, in enzyme yield was observed. Economic enzyme production by immobilized B. circulans is regulated by interactive influence of fermentation parameters, which influence the immobilized bead stability, reusability, and enzyme yield.

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“…3.1.1.3), which catalyse the hydrolysis of triglycerides, are among the most promising to be used in detergents. Several studies have shown the beneficial effects of lipases for the elimination of dirt adhering to fabrics, most notably the increase in detergency at low temperatures [2][3][4][5].…”

Section: Introductionmentioning

confidence: 99%

Hard‐Surface Cleaning Using Lipases: Enzyme–Surfactant Interactions and Washing Tests

Jurado

Bravo

Luzón

et al. 2007

J Surfact & Detergents

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A commercial lipase (E.C. 3.1.1.3) from Thermomyces lanuginosus was studied in order to assess its interaction with commercial nonionic (Findet Ò 1214N/16, Findet 1214N/23 and Glucopon Ò 650) and anionic (linear alkylbenzene sulphonate; LAS) surfactants, as well as the cleaning action exerted by the enzyme on hard surfaces. Nonionic surfactants seem to prevent or delay enzyme penetration at the interface, thereby decreasing lipase activity. Notably, no inhibitory effect of the anionic surfactant LAS on lipase action was found, higher conversions being achieved after 20 min of enzymatic hydrolysis in the presence of this surfactant than in its absence. A device for testing detersive performance, the so-called bath-substrateflow, was used in washing experiments with the lipase at different temperatures with or without surfactant. Employing two different oily stains (tributyrin and triolein), it was found that the lipase by itself increases detergency significantly, preventing the subsequent redeposition of the removed dirt. Expressions relating detersive efficiency to lipase concentration and temperature were obtained using ''Statistical Design of Experiments'' methodology.

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Mechanistic studies of proteases and lipases for the detergent industry

Abstract: A B S T R A C TThe wash performance of three specific proteases (asp, lysfarg and glu specific, respectively)

Cited by 51 publications

References 1 publication

Overview of Fungal Lipase: A Review

Overview of Fungal Lipase: A Review

Studies on Improving the Immobilized Bead Reusability and Alkaline Protease Production by Isolated Immobilized Bacillus circulans (MTCC 6811) Using Overall Evaluation Criteria

Hard‐Surface Cleaning Using Lipases: Enzyme–Surfactant Interactions and Washing Tests

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