A structural model of mono- and diacylglycerol lipase from Penicillium camembertii

Isobe, Kimiyasu; Aumann, Klaus-Dieter; Schmid, Rolf D.

doi:10.1016/0168-1656(94)90123-6

Cited by 14 publications

(7 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The value obtained for P. solitum 194A was in line with the most well-known lipases from the genus Penicillium (a molecular mass in the range of 25-43 kDa), 29,34) similar to the value obtained for the type II lipases from P. camembertii (38 kDa) 5,35,36) and P. cyclopium (40-43 kDa). 5,35) Conversely, the value differed from the molecular mass of the type I P. solitum lipase previously reported (27 kDa).…”

Section: Discussionsupporting

confidence: 66%

Biochemistry of lipolytic enzymes secreted byPenicillium solitumandCladosporium cladosporioides

Chinaglia

Chiarelli

Maggi

et al. 2014

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Two distinct extracellular lipases were obtained from Penicillium solitum 194A, isolated from domestic compost, and Cladosporium cladosporioides 194B, isolated from dairy wastewater. These alkaline enzymes had molecular masses of 42 and 30 kDa, respectively. The P. solitum 194A lipase differed in mass from previously reported enzyme, indicating that it is a novel lipase, and indicating that penicillia can secrete lipase isoenzymes. The C. cladosporioides lipase was more active on esters of medium-chain acids, whereas the P. solitum lipase was more active on longer chained substrates. The C. cladosporioides enzyme displayed higher thermal stability than the P. solitum lipase, preserving full activity up to 48 °C and showing a T50 (10 min) of 60 °C. Their different catalytic properties and good protein stability should make these enzymes suitable for biotechnological applications. Furthermore, the combined use of these two fungal strains may prove to be valuable in lipid-rich waste management.

show abstract

Section: Discussionsupporting

confidence: 66%

Biochemistry of lipolytic enzymes secreted byPenicillium solitumandCladosporium cladosporioides

Chinaglia

Chiarelli

Maggi

et al. 2014

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

show abstract

“…A lipase from P. camembertii U-150 was purified into four active fractions by a procedure involving ammonium sulfate fractionation, ethanol precipitation and aminooctyl-Sepharose, hydroxyapatite, and Con A-Sepharose column chromatographies [214]. However, a novel enzyme hydrolysing mono-and diglycerols was found in the culture filtrate of P. camembertii U-150 by Yamaguchi and Mase [215].…”

Section: Purificationmentioning

confidence: 98%

Overview of Fungal Lipase: A Review

Singh

Mukhopadhyay

2011

Appl Biochem Biotechnol

343

200

View full text Add to dashboard Cite

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.

show abstract

“…H257 [21] and fungus Malassezia globosa [22] have been reported, and yet, little has been known about structural basis accounting for their unique substrate selectivity. A simple structural model of PCL was described by Isobe et al, in which the substrate selectivity of PCL was loosely correlated to the distance between the carboxyl carbon of substrates and the nucleophilic O␥ of Ser145 [23]. Based on its crystal structure, the mechanism of substrate selectivity of MDGL from Malassezia globosa (SMG1) was investigated in detail [22,24].…”

Section: Introductionmentioning

confidence: 99%

A “bridge-like” structure responsible for the substrate selectivity of mono- and diacylglycerol lipase from Aspergillus oryzae

Liu

Lan

Wang

et al. 2013

Journal of Molecular Catalysis B: Enzymatic

View full text Add to dashboard Cite

A structural model of mono- and diacylglycerol lipase from Penicillium camembertii

Cited by 14 publications

References 15 publications

Biochemistry of lipolytic enzymes secreted byPenicillium solitumandCladosporium cladosporioides

Biochemistry of lipolytic enzymes secreted byPenicillium solitumandCladosporium cladosporioides

Overview of Fungal Lipase: A Review

A “bridge-like” structure responsible for the substrate selectivity of mono- and diacylglycerol lipase from Aspergillus oryzae

Contact Info

Product

Resources

About