Present and Future Applications of Lipases

Macrae, Alasdair R.; Hammond, Roger

doi:10.1080/02648725.1985.10647813

Cited by 291 publications

(128 citation statements)

References 80 publications

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“…A produção de lipase por Geotrichum candidum tem sido amplamente relatada na literatura, dada sua especificidade de hidrólise de acilgliceróis contendo ácidos graxos de cadeia longa com dupla ligação na posição 9 [30][31][32] . Os valores de atividade do extrato enzimático bruto obtidos desta cepa (12,8 U/mL), assim como sua atividade específica (0,42 U/mg), foram praticamente o dobro dos valores relatados para o extrato bruto de uma cepa de Geotrichum sp (6,22 U/mL e 0,23 U/mg, respectivamente), após fermentação em meio líquido composto de farinha de soja e trigo em pó como fontes de carbono e extrato de levedura e NH 4 NO 3 como fontes de nitrogênio 33 .…”

Section: Resultados E Discussão Produção Das Enzimas E Atividades Enzunclassified

Potencial de biocatálise enantiosseletiva de lipases microbianas

Carvalho¹,

Calafatti²,

Marassi³

et al. 2005

Quím. Nova

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Recebido em 18/5/04; aceito em 12/11/04; publicado na web em 13/4/05 POTENTIAL OF ENANTIOSELECTIVE BIOCATALYSIS BY MICROBIAL LIPASES. Microbial lipases have a great potential for commercial applications due to their stability, selectivity and broad substrate specificity because many non-natural acids, alcohols or amines can be used as the substrate. Three microbial lipases isolated from Brazilian soil samples (Aspergillus niger; Geotrichum candidum; Penicillium solitum) were compared in terms of their stability and as biocatalysts in the enantioselective esterification using racemic substrates in organic medium. The lipase from Aspergillus niger showed the highest activity (18.2 U/mL) and was highly thermostable, retaining 90% and 60% activity at 50 o C and 60 o C after 1 hour, respectively. In organic medium, this lipase provided the best results in terms of enantiomeric excess of the (S)-active acid (ee = 6.1%) and conversion value (c = 20%) in the esterification of (R,S)-ibuprofen with 1-propanol in isooctane. The esterification reaction of the racemic mixture of (R,S)-2-octanol with decanoic acid proceeded with high enantioselectivity when lipase from Aspergillus niger (E = 13.2) and commercial lipase from Candida antarctica (E = 20) were employed.Keywords: lipases; enantioselectivity; (R,S)-ibuprofen. INTRODUÇÃOA biocatálise é hoje um dos campos mais promissores dentro das novas tecnologias para síntese de compostos de alto valor agregado. A exploração da biodiversidade na busca de novos catalisadores por técnicas de seleção de microrganismos, de plantas ou células animais representam os métodos tradicionais de descoberta de novas enzimas para o desenvolvimento da biocatálise em escala industrial 1 . Os microrganismos neste caso são de particular interesse devido ao curto período de geração, à grande diversidade de processos metabólicos e enzimas envolvidas e, não há um número limitado de microrganismos na natureza que possam ser testados, os quais são bastante diferentes entre si. Microrganismos isolados em território brasileiro têm demonstrado excelente potencial biocatalisador frente a diferentes substratos orgânicos de interesse, como por ex. na hidrólise de óleos marinhos 2,3 , na síntese de ésteres de ácidos graxos poliinsaturados 4 e de ésteres de aroma 5 .Dentre as enzimas hidrolíticas de maior interesse estão as lipases (glicerol ester hidrolase E C. 3.1.1.3), que são biocatalisadores versáteis capazes de catalisar diferentes reações, tanto em meio aquoso como em meio orgânico, com teor de água restrito. Entre as lipases de vegetais, animais e microbianas, estas últimas são as mais utilizadas e, na sua grande maioria, não são nocivas a saúde humana, sendo reconhecidas como "Generally Regarded as Save -GRAS" 6 . Do ponto de vista industrial, os fungos são especialmente valorizados porque as enzimas por eles produzidas normalmente são extracelulares, o que facilita sua recuperação do meio de fermentação 7 . Os trabalhos replatados em literatura sobre lipases fúngicas são numerosos, sendo que os mais ...

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Section: Resultados E Discussão Produção Das Enzimas E Atividades Enzunclassified

Potencial de biocatálise enantiosseletiva de lipases microbianas

Carvalho¹,

Calafatti²,

Marassi³

et al. 2005

Quím. Nova

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“…Further, this observation also indicated that this enzyme may probably act synergistically to hydrolyze extracellular lipids to free fatty acids and glycerols. In fact most of the bacterial lipases reported so far are constitutive and are non-specific in their substrate specificity (Macrae and Hammond 1985). The majority of enzymes require the presence of metal ion activators to express their full catalytic activity, and thus metal ion activation of enzyme reactions is important in industrial applications for achieving maximal catalytic efficiency and a number of enzymes require the presence of metal ions, such as calcium ions, for the maintenance of their stable and active structures (Gray 1995).…”

Section: Discussionmentioning

confidence: 99%

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

Lailaja

Chandrasekaran

2013

World J Microbiol Biotechnol

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Bacillus smithii BTMS 11, isolated from marine sediment, produced alkaline and thermostable lipase. The enzyme was purified to homogeneity by ammonium sulfate precipitation and ion exchange chromatography which resulted in 0.51 % final yield and a 4.33 fold of purification. The purified enzyme was found to have a specific activity of 360 IU/mg protein. SDS-PAGE analyses, under non-reducing and reducing conditions, yielded a single band of 45 kDa indicating the single polypeptide nature of the enzyme and zymogram analysis using methylumbelliferyl butyrate as substrate confirmed the lipolytic activity of the protein band. The enzyme was found to have 50°C and pH 8.0 as optimum conditions for maximal activity. However, the enzyme was active over wide range of temperatures (30-80°C) and pH (7.0-10.0). Effect of a number of metal salts, solvents, surfactants, and other typical enzyme inhibitors on lipase activity was studied to determine the novel characteristics of the enzyme. More than 90 % of the enzyme activity was observed even after 3 h of incubation in the presence of commercial detergents Surf, Sunlight, Ariel, Henko, Tide and Ujala indicating the detergent compatibility of B. smithii lipase. The enzyme was also found to be efficient in stain removal from cotton cloths. Further it was observed that the enzyme could catalyse ester synthesis between fatty acids of varying carbon chain lengths and methanol with high preference for medium to long chain fatty acids showing 70 % of esterification. Results of the study indicated scope for application of this marine bacterial lipase in various industries.

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“…(Paques and Macedo, 2006) According to Villeneuve (2003), Macrae and Hammond (1985) and Sonnet (1988), lipase specificities can be divided into three main groups as follows:…”

Section: Brazilian Journal Of Chemical Engineeringmentioning

confidence: 99%

Seed lipases: sources, applications and properties - a review

Barros

Fleuri

Macêdo

2010

Braz. J. Chem. Eng.

178

100

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-This paper provides an overview regarding the main aspects of seed lipases, such as the reactions catalyzed, physiological functions, specificities, sources and applications. Lipases are ubiquitous in nature and are produced by several plants, animals and microorganisms. These enzymes exhibit several very interesting features, such as low cost and easy purification, which make their commercial exploitation as industrial enzymes a potentially attractive alternative. The applications of lipases in food, detergents, oils and fats, medicines and fine chemistry, effluent treatment, biodiesel production and in the cellulose pulp industry, as well as the main sources of oilseed and cereal seed lipases, are reviewed.

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Present and Future Applications of Lipases

Cited by 291 publications

References 80 publications

Potencial de biocatálise enantiosseletiva de lipases microbianas

Potencial de biocatálise enantiosseletiva de lipases microbianas

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

Seed lipases: sources, applications and properties - a review

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