Substrate-Specificity of<i>Candida rugosa</i>Lipase and Its Industrial Application

Vanleeuw, Evelien; Winderickx, Sofie; Thevissen, Karin; Lagrain, Bert; Dusselier, Michiel; Cammue, Bruno P. A.; Sels, Bert F.

doi:10.1021/acssuschemeng.9b03257

Cited by 70 publications

(41 citation statements)

References 140 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…On the other hand, lipase is inactive when its lid is closed 6 . The use of lipases as a biocatalyst has advantages of high selectivity and specificity, in addition to being able to maintain catalytic activity in aqueous and nonaqueous solutions 7,8 . Thus, lipases have been very attractive for numerous industrial applications, 9 such as pharmaceuticals, 10 fatty acids, 11 biofuels, 12 and food 13 .…”

Section: Introductionmentioning

confidence: 99%

“…6 The use of lipases as a biocatalyst has advantages of high selectivity and specificity, in addition to being able to maintain catalytic activity in aqueous and nonaqueous solutions. 7,8 Thus, lipases have been very attractive for numerous industrial applications, 9 such as pharmaceuticals, 10 fatty acids, 11 biofuels, 12 and food. 13 For this reasons, the use of these biocatalysts is a very promising alternative for developing environmentally friendly processes.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Brandão

Barbosa

Souza

et al. 2020

Biotechnology Progress

View full text Add to dashboard Cite

Bioimprinting is an easy, sustainable and low-cost technique that promotes a printing of potential substrates on enzyme structure, inducing a more selective and stable conformation. Bioimprinting promotes conformational changes in enzymes, resulting in better catalytic performance. In this work, the effect of bioimprinting of Burkholderia cepacia lipase (BCL) and porcine pancreatic extracts (PPE) with four different fatty acids (lauric acid (C12:0), myristic acid (C14:0), palmitic acid (C16:0), and stearic acid (C18:0)) was investigated. The results demonstrated that the better bioimprinting effect was in BCL with lauric acid in esterification reaction, promoting BCL activation in which relative enzyme activity was 70 times greater than nonimprinted BCL. Bioimprinting results were influenced by the carbon chain length of fatty acids imprinted in the BCL, in which the effects were weaker with the chain increase. Molecular docking was performed to better understand the bioimprinting method. The results of these simulations showed that indeed all fatty acids were imprinted in the active site of BCL. However, lauric acid presented the highest imprinting preference in the active site of BCL, resulting in the highest relative activity. Furthermore, Fourier transform infrared (FTIR) analysis confirmed important variations in secondary structure of bioimprinting BCL with lauric acid, in which there was a reduction in the α-helix content and an increase in the β-sheet content that facilitated substrate access to the active site of BCL and led higher rigidity, resulting in high activity. Bioimprinted BCL with lauric acid showed excellent operational stability in esterification reaction, maintaining its original relative activity after five successive cycles. Thus, the results show that bioimprinting of BCL with lauric acid is a successful strategy due to its high catalytic activity and reusability.

show abstract

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Brandão

Barbosa

Souza

et al. 2020

Biotechnology Progress

View full text Add to dashboard Cite

show abstract

“…Candida species can express eight LIP gene family with a high amino acid identity and similarity among them [5]. In these work, CvLIP4 from C. viswanathii was identify among homologous sequence from Candida species and degenerated primers were designed and analyzed in different carbon sources.…”

Section: Discussionmentioning

confidence: 99%

“…The differences in substrate specificity may be related to specific amino acid variations in the different parts that compose the catalytic machinery. The commercial CRL is actually a mixture of three Lip isoenzymes (Lip1, Lip2, Lip3) present in different proportions (e.g., the CRL mixture of Sigma is composed of 73% Lip1, 8% Lip2 and 19% Lip3) with Lip1 being the major component [5].…”

Section: Introductionmentioning

confidence: 99%

LIP4 gene expression from Candida viswanathii strain

Rc¹,

Mm²,

NMLd³

et al. 2020

Preprint

View full text Add to dashboard Cite

Background : Lipases are hydrolases that catalyze the cleavage of triglyceride esters bonds, releasing glycerol and free fatty acids. Candida genus can produce distinct isoforms of lipase, among of them, Candida viswanathii strain is a potential lipase producer using hydrophobic carbons sources in which produced high level of enzyme under submerged cultivation using olive oil as carbon sources. This enzyme has commercially attractive due to characteristics desired in the industries processes. The genes responsible for encoding the lipases comprise a family called LIP gene. C. viswanathii not have its genome sequenced and are not available in annotated form through the GenBank nucleotide sequence database for lipase production. The aim of this work was understanding at molecular level the effect of carbon sources to lipase production, to identify and to analyses the gene expression of CvLIP4 from C. viswanathii on different culture media. Results : In silico analysis was carried out with LIP4 gene from Candida species. Degenerate primers were designed and evaluated for expression in different conditions. CvLIP4 expression was evaluated using carbon sources glucose, tributyrin, triolein and olive oil. Triolein and olive oil were strong inducer for CvLIP4 gene expression, while tributyrin was a weak inducer and glucose was strong repressor. Conclusions : These results will contribute to further studies about regulation of the lipase genes expression from C. viswanathii and heterologous expression of this enzyme to improve the catalytic conditions in industries processes.

show abstract

“…The microbial lipases in the form of powder is projected to dominate the microbial lipase markets due to its stability, easy to handle, and easier for packaging and its transportation preferred by the consumers [ 21 , 22 ]. These are extensively applicable in several another industries such as dairy, food and beverage, animal feed, cleaning, biofuel, pharmaceuticals, textile cosmetic, perfumery, flavour industry, biocatalytic resolution, esters and amino acid derivatives, fine chemicals production, agrochemicals, biosensor, and bioremediation [ 23 – 25 ]. Additionally, altering in the dietary patterns have led to augmented the consumption of dairy products in the region; increasing in trepidations about superior hygiene, in consciousness of personal hygiene, contagious diseases, and bleaching household industrial surfaces [ 26 ].…”

Section: Introductionmentioning

confidence: 99%

Microbial lipases and their industrial applications: a comprehensive review

et al. 2020

View full text Add to dashboard Cite

Lipases are very versatile enzymes, and produced the attention of the several industrial processes. Lipase can be achieved from several sources, animal, vegetable, and microbiological. The uses of microbial lipase market is estimated to be USD 425.0 Million in 2018 and it is projected to reach USD 590.2 Million by 2023, growing at a CAGR of 6.8% from 2018. Microbial lipases (EC 3.1.1.3) catalyze the hydrolysis of long chain triglycerides. The microbial origins of lipase enzymes are logically dynamic and proficient also have an extensive range of industrial uses with the manufacturing of altered molecules. The unique lipase (triacylglycerol acyl hydrolase) enzymes catalyzed the hydrolysis, esterification and alcoholysis reactions. Immobilization has made the use of microbial lipases accomplish its best performance and hence suitable for several reactions and need to enhance aroma to the immobilization processes. Immobilized enzymes depend on the immobilization technique and the carrier type. The choice of the carrier concerns usually the biocompatibility, chemical and thermal stability, and insolubility under reaction conditions, capability of easy rejuvenation and reusability, as well as cost proficiency. Bacillus spp., Achromobacter spp., Alcaligenes spp., Arthrobacter spp., Pseudomonos spp., of bacteria and Penicillium spp., Fusarium spp., Aspergillus spp., of fungi are screened large scale for lipase production. Lipases as multipurpose biological catalyst has given a favorable vision in meeting the needs for several industries such as biodiesel, foods and drinks, leather, textile, detergents, pharmaceuticals and medicals. This review represents a discussion on microbial sources of lipases, immobilization methods increased productivity at market profitability and reduce logistical liability on the environment and user.

show abstract

Substrate-Specificity ofCandida rugosaLipase and Its Industrial Application

Cited by 70 publications

References 140 publications

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

LIP4 gene expression from Candida viswanathii strain

Microbial lipases and their industrial applications: a comprehensive review

Contact Info

Product

Resources

About