Active center and enzymatic properties of esterase produced by Lichtheimia sp
Pages 575 - 580
Abstract
The structure of Lichtheimia sp. esterase active center and its modification kinetics were studied by chemical modification method. The results showed that PMSF and mercaptoethanol could significantly inhibit the enzyme activity. The active center of PMSF consisted of at least one serine residue and one cysteine residue. Bromoacetic acid, n-acetylimidazole, acetylacetone, chloramine-T and N-bromosuccinimide had no significant inhibition on the enzyme activity, while histidine, tyrosine, arginine, methionine, tryptophan and tryptophan might be the essential groups of the enzyme activity center. The inhibitory effect of EDTA was more obvious, followed by β -mercaptoethanol. SDS surfactant had strong inhibitory effect on esterase production, and Twain -80 and Twain -60 had the same inhibitory effect on esterase production. Organic solvent can promote esterification enzyme production. Isopropyl alcohol has the most obvious promoting effect, followed by methanol, butanol has no obvious promoting effect.
References
[1]
Contesinia F J, Lopesa D B, Macedoa C A, et al. Aspergillus sp. lipase: potential biocatalyst for industrial use [J]. Journal of Molecular Catalysis B: Enzymatic, 2010, 67, (3-4): 163--171
[2]
M.Chen, et al., The effects of two chemical modifiers on the activity and stability of wheat esterase[J]. Food Science, 2013(21):167--171.
[3]
X.H.Lin, Study on fermentation conditions of α-glucosidase produced by Aspergillus niger[J]. Modern Food, 2018, (5): 48--51.
[4]
H.Y.Wang, et al., Chemical modification of peroxidase functional groups in water spinach leaves[J]. Journal of Food and Biotechnology, 2016, 35(02):192--196.
[5]
J.P.Wang, et al., The catalytic domain structure and key amino acid analysis of 4-α-glycosyltransferase[J]. Journal of Food Science and Biotechnology, 2013 (32):06.
[6]
H.P.Han, L.Q.Zhang, Chemical modification of cellulase produced by actinomycetes[J]. Food Science, 2012-04-27.
[7]
E.Li, X.T.Li, Chemical modification and active center of xylanase from Streptomyces cladosus L2001[J]. Chinese Journal of Food Science, 2012(1): 25--31.
Index Terms
- Active center and enzymatic properties of esterase produced by Lichtheimia sp
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October 2021
593 pages
ISBN:9781450395588
DOI:10.1145/3500931
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Association for Computing Machinery
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Published: 22 December 2021
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ISAIMS 2021
ISAIMS 2021: 2nd International Symposium on Artificial Intelligence for Medicine Sciences
October 29 - 31, 2021
Beijing, China
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Overall Acceptance Rate 53 of 112 submissions, 47%
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