Esterase Active in Polar Organic Solvents from the Yeast Pseudozyma sp. NII 08165

Esterases/lipases active in water miscible solvents are highly desired in biocatalysis where substrate solubility is limited and also when the solvent is desired as an acyl acceptor in transesterification reactions, as with the case of biodiesel production. We have isolated an esterase from the glycolipid producing yeast-Pseudozyma sp. NII 08165 which in its crude form was alkali active, thermo stable, halo tolerant and also capable of acting in presence of high methanol concentration. The crude enzyme which maintained 90% of its original activity after being treated at 70°C was purified and the properties were characterized. The partially purified esterase preparation had temperature and pH optima of 60°C and 8.0 respectively. The enzyme retained almost complete activity in presence of 25% methanol and 80% activity in the same strength of ethanol. Conditions of enzyme production were optimized, which lead to 9 fold increase in the esterase yield. One of the isoforms of the enzyme LIP1 was purified to homogeneity and characterized. Purified LIP1 had a Km and Vmax of 0.01 and 1.12, respectively. The purified esterase lost its thermo and halo tolerance but interestingly, retained 97% activity in methanol.

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Analysis of natural wax from Nelumbo nucifera leaves by using polar and non-polar organic solvents

Process Biochemistry ◽

10.1016/j.procbio.2021.04.007 ◽

2021 ◽

Author(s):

Aradhya Dev Srivastav ◽

Vireshwar Singh ◽

Deepak Singh ◽

Balendu Shekher Giri ◽

Dhananjay Singh

Keyword(s):

Organic Solvents ◽

Nelumbo Nucifera ◽

Polar Organic Solvents ◽

Natural Wax

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β-Galactosidase-Producing Isolates in Mucoromycota: Screening, Enzyme Production, and Applications for Functional Oligosaccharide Synthesis

Journal of Fungi ◽

10.3390/jof7030229 ◽

2021 ◽

Vol 7 (3) ◽

pp. 229

Author(s):

Bettina Volford ◽

Mónika Varga ◽

András Szekeres ◽

Alexandra Kotogán ◽

Gábor Nagy ◽

...

Keyword(s):

Wheat Bran ◽

Enzyme Production ◽

Specific Activity ◽

Prebiotic Synthesis ◽

Crude Enzyme ◽

Oligosaccharide Synthesis ◽

Industrial Enzymes ◽

Chromogenic Agar ◽

Lichtheimia Ramosa ◽

Excellent Source

β-Galactosidases of Mucoromycota are rarely studied, although this group of filamentous fungi is an excellent source of many industrial enzymes. In this study, 99 isolates from the genera Lichtheimia, Mortierella, Mucor, Rhizomucor, Rhizopus and Umbelopsis, were screened for their β-galactosidase activity using a chromogenic agar approach. Ten isolates from the best producers were selected, and the activity was further investigated in submerged (SmF) and solid-state (SSF) fermentation systems containing lactose and/or wheat bran substrates as enzyme production inducers. Wheat bran proved to be efficient for the enzyme production under both SmF and SSF conditions, giving maximum specific activity yields from 32 to 12,064 U/mg protein and from 783 to 22,720 U/mg protein, respectively. Oligosaccharide synthesis tests revealed the suitability of crude β-galactosidases from Lichtheimia ramosa Szeged Microbiological Collection (SZMC) 11360 and Rhizomucor pusillus SZMC 11025 to catalyze transgalactosylation reactions. In addition, the crude enzyme extracts had transfructosylation activity, resulting in the formation of fructo-oligosaccharide molecules in a sucrose-containing environment. The maximal oligosaccharide concentration varied between 0.0158 and 2.236 g/L depending on the crude enzyme and the initial material. Some oligosaccharide-enriched mixtures supported the growth of probiotics, indicating the potential of the studied enzyme extracts in future prebiotic synthesis processes.

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Dissolution of oxidation-cured poly(carbosilane) fiber into polar organic solvents

Journal of Applied Polymer Science ◽

10.1002/(sici)1097-4628(19970711)65:2<261::aid-app6>3.0.co;2-m ◽

1997 ◽

Vol 65 (2) ◽

pp. 261-265 ◽

Cited By ~ 2

Author(s):

Masaki Narisawa ◽

Satoshi Oda ◽

Shuhei Kitano ◽

Kiyohito Okamura

Keyword(s):

Organic Solvents ◽

Polar Organic Solvents

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Production and Properties of a Bacterial Thermostable Exo-inulinase

Zeitschrift für Naturforschung C ◽

10.1515/znc-2001-11-1220 ◽

2001 ◽

Vol 56 (11-12) ◽

pp. 1022-1028 ◽

Cited By ~ 7

Author(s):

Kristina Uzunova ◽

Anna Vassileva ◽

Margarita Kambourova ◽

Viara Ivanova ◽

Dimitrina Spasova ◽

...

Keyword(s):

Enzyme Production ◽

Enzyme Preparation ◽

Batch Cultivation ◽

Crude Enzyme ◽

Growth Time ◽

Bacillus Sp ◽

High Thermostability ◽

Crude Enzyme Preparation ◽

Ph Range

Abstract Enzyme production of newly isolated thermophilic inulin-degrading Bacillus sp. 11 strain was studied by batch cultivation in a fermentor. The achieved inulinase and invertase activi ties after a short growth time (4.25 h) were similar or higher compared to those reported for other mesophilic aerobic or anaerobic thermophilic bacterial producers and yeasts. The investigated enzyme belonged to the exo-type inulinases and splitted-off inulin, sucrose and raffinose. It could be used at temperatures above 65 °C and pH range 5.5-7.5. The obtained crude enzyme preparation possessed high thermostability. The residual inulinase and inver tase activities were 92-98% after pretreatment at 65 °C for 60 min in the presence of substrate inulin.

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