The Extracellular Lipases of Some Gram-Negative Non-Sporeforming Rod-Shaped Bacteria

Nashif, S.A.; Nelson, F. E.

doi:10.3168/jds.s0022-0302(53)91549-5

Cited by 17 publications

(4 citation statements)

References 7 publications

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“…B. coli communis (Escherichia coli) was found to be lipase negative (34). Only a few lipase-producing bacteria were further characterized (95), but research was intensified when it became generally accepted that lipases remain enzymatically active in organic solvents (166), making them ideal tools for the organic chemist. The aim of this review is not to discuss every lipase described in the literature but rather to present recent information on selected and novel lipases.…”

Section: ? Introductionmentioning

confidence: 99%

Bacterial Biocatalysts: Molecular Biology, Three-Dimensional Structures, and Biotechnological Applications of Lipases

Jaeger

Dijkstra

Reetz

1999

Annu. Rev. Microbiol.

979

696

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Bacteria produce and secrete lipases, which can catalyze both the hydrolysis and the synthesis of long-chain acylglycerols. These reactions usually proceed with high regioselectivity and enantioselectivity, and, therefore, lipases have become very important stereoselective biocatalysts used in organic chemistry. High-level production of these biocatalysts requires the understanding of the mechanisms underlying gene expression, folding, and secretion. Transcription of lipase genes may be regulated by quorum sensing and two-component systems; secretion can proceed either via the Sec-dependent general secretory pathway or via ABC transporters. In addition, some lipases need folding catalysts such as the lipase-specific foldases and disulfide-bond-forming proteins to achieve a secretion-competent conformation. Three-dimensional structures of bacterial lipases were solved to understand the catalytic mechanism of lipase reactions. Structural characteristics include an alpha/beta hydrolase fold, a catalytic triad consisting of a nucleophilic serine located in a highly conserved Gly-X-Ser-X-Gly pentapeptide, and an aspartate or glutamate residue that is hydrogen bonded to a histidine. Four substrate binding pockets were identified for triglycerides: an oxyanion hole and three pockets accommodating the fatty acids bound at position sn-1, sn-2, and sn-3. The differences in size and the hydrophilicity/hydrophobicity of these pockets determine the enantiopreference of a lipase. The understanding of structure-function relationships will enable researchers to tailor new lipases for biotechnological applications. At the same time, directed evolution in combination with appropriate screening systems will be used extensively as a novel approach to develop lipases with high stability and enantioselectivity.

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Section: ? Introductionmentioning

confidence: 99%

Bacterial Biocatalysts: Molecular Biology, Three-Dimensional Structures, and Biotechnological Applications of Lipases

Jaeger

Dijkstra

Reetz

1999

Annu. Rev. Microbiol.

979

696

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“…The importance of lipolytic activity of microorganisms in meats, meat products, and dairy products held at low temperatures has been recognized for many years (5,6,7,9). Although there have been numerous investigations on various factors affecting the production of lipase by microorganisms, only a few have been concerned with the effects of temperature, Nashif and Nelson (10) found that Pseudomonas frag; had an optimum temperature around 15" C for lipase production and that several other Gram-negative bacteria produced maximum quantities of lipase around 20" C even though the optimum temperature for activity of the lipases was near 40" C (12). Greene and Jezeski (5) reported a close correlation between total bacterial counts and onset of lipolytic activity by a Pseudomonas species over a temperature range of 0" to 30" C.…”

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confidence: 99%

LIPOLYTIC ACTIVITY OF MICROORGANISMS AT LOW AND INTERMEDIATE TEMPERATURES. I. ACTION OF PSEUDOMONAS FLUORESCENS ON LARD^a

Alford

Elliott

1960

Journal of Food Science

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“…It is important, fro the cheese-flavor development stand point, that the raw milk lipase e.g. Pseudomonas fragi [49] with stood a heat treatment at 62 or 72 °C for 30 min. The lipase complete inactivation ha s heat required at 66 °C for 1 hour and 70 °C for ten min [50,51].…”

Section: Cheese Ripeningmentioning

confidence: 99%

Lipases, Definition, and their Application

Moayd¹,

Yan²

2017

IOSRJPBS

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Esterase and lipase have been consisted of α/β hydroxylase super family that characterized primarily by their α/β hydroxylase fold (common fold), which is in the center, pre-dominantly parallel β-sheet and flanked via the connections of α-helical. Nucleophilic elbow is an esterases and lipases that shared the characteristic sequence motifs (GXSXG I. Lipase and Esterase DefinitionEstarase and lipase are cosisted of α/β hydroxylase super famliy that characterized primarily by their α/β hydroxylase fold (common fold), which is in the center, pre-dominantly parallel β-sheet and flanked via the connections of α-helical. Nucleophilic elbow is esterases and lipases that shared the characteristic sequence motifs (GXSXG) [1,2]. This motif is embeded by serine, and the mediation of ester hydrolysis by attacking the nucleophilic of serine active on the substrate carbonyl in the system of a charge relay with other two residues of amino acid (histidine and aspartic acid) [1]. The residues of these amino acids compose a triad of catalyse in the specific-order (serine -aspartic acid -histidine) in the chain of polypeptide [3][4][5][6]. Forthat, the most of lipases and esterases resemble serine-proteases and lipases in hydrolytic mechanims. Esterases (EC 3.1.1.1), as well as lipases (EC 3.1.1.3)are the versatile classes of biocatalysts due to their region-, enatio-selectivity and high specificity. Esterases are those that can catalyze the hydrolysis of less than 10 short-acyl-chain-lengthed triglycerides, whereas, lipases are catalysts that can hydrolyze more than 10 long-acyl-chain-lengthed triglycerides. Studies of the structure displayed that the presene or absence of lid structure caused the diffrentiation between esterases and lipases and responsible for lipase interfacial activation [4][5][6][7]. Life kindoms has a widely distribution from esterase and lipases.In a widly ranging from organisms, esterases and lipases have been identified and cloned severel of them. Acinetobacter [8,9], Bacillus [10,11] and Pseudomonas [12,13] are examples from various microbial strains that possess identifing and cloning of esterases and lipases. The studies have been reported that, metal ions and organic solvent resistance related to microbial esterases and lipases [14]. Thus, they should be catalysis effeceintly in organic synthisis for an enantio-and regionselective reactions, among the groups biocatalysis that have been the most important in biotechnology. The optically pure substances in organic synthesis have been used esterases and lipases successfully. II. Lipase applicationLipases applications can be widely produced from a bacterial and fungal production. In fact, they have stability in organic solvent wide range and many present high thermostabilities, they have optimal range of temperature and wider pH than eukaryotic origin lipases, and have a high diverse range of substrate with high enantio-and regioselectivity making an important microbial lipases and attractive choice in organic synthesis for many applications. Li...

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The Extracellular Lipases of Some Gram-Negative Non-Sporeforming Rod-Shaped Bacteria

Cited by 17 publications

References 7 publications

Bacterial Biocatalysts: Molecular Biology, Three-Dimensional Structures, and Biotechnological Applications of Lipases

Bacterial Biocatalysts: Molecular Biology, Three-Dimensional Structures, and Biotechnological Applications of Lipases

LIPOLYTIC ACTIVITY OF MICROORGANISMS AT LOW AND INTERMEDIATE TEMPERATURES. I. ACTION OF PSEUDOMONAS FLUORESCENS ON LARD^a

Lipases, Definition, and their Application

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The Extracellular Lipases of Some Gram-Negative Non-Sporeforming Rod-Shaped Bacteria

Cited by 17 publications

References 7 publications

Bacterial Biocatalysts: Molecular Biology, Three-Dimensional Structures, and Biotechnological Applications of Lipases

Bacterial Biocatalysts: Molecular Biology, Three-Dimensional Structures, and Biotechnological Applications of Lipases

LIPOLYTIC ACTIVITY OF MICROORGANISMS AT LOW AND INTERMEDIATE TEMPERATURES. I. ACTION OF PSEUDOMONAS FLUORESCENS ON LARDa

Lipases, Definition, and their Application

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Product

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LIPOLYTIC ACTIVITY OF MICROORGANISMS AT LOW AND INTERMEDIATE TEMPERATURES. I. ACTION OF PSEUDOMONAS FLUORESCENS ON LARD^a