NDLI: The Effect of pH on Globular State of Lipase-3646; an Appropriate Model for Molten Globule Investigations.

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The Effect of pH on Globular State of Lipase-3646; an Appropriate Model for Molten Globule Investigations.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Golaki, Bahram Pooreydy Aminzadeh, Saeed Karkhane, Ali Asghar Yakhchali, Bagher Farrokh, Parisa Jazii, Ferdous Rastgar Nadimifar, Mohammadsadegh
Description	Country affiliation: Iran Author Affiliation: Golaki BP ( Bioprocess Engineering Group, Department of Industrial and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB), Sharek-e Pajoohesh Km 15, Tehran-Karaj Highway, P.O. Box: 14965/161, Tehran, Iran.)
Abstract	Secondary structure content of proteins in molten globule state is relatively constant while the quantity of tertiary structures clearly declines due to alterations in side-chain packing. In the present study, we analyze the MG state of lipase-3646 for the first time. We introduce lipase-3646 as an appropriate model for investigating the properties and behavior of a protein in MG state as well as folding pathway. Applying fluorescence spectroscopy we measured both intrinsic and extrinsic fluorescence of lipase-3646 in a pH range from 1.0 to 12.0. It was found that at pH 3.0 the protein acquires a MG state. Applying far-UV circular dichroism (CD), our analysis on the secondary structure of lipase-3646 revealed a slight change in the MG state intermediate (pH 3.0) compared to the native state (pH 8.5), which this amount of change is common for MG. Measurements in near-UV CD also showed a significant change in the enzyme conformation at pH 3.0 in comparison with the pH 8.5 wherein the protein acquires its native structure. Quenching the fluorescence by applying acrylamide, the amount 23 and 35 M(-1) were measured at pHs 8.5 and 3.0 respectively for stern-volmer constant (KSV). An increase in the enzyme molecular volume in the MG state was confirmed by gel filtration chromatography.
File Format	HTM / HTML
ISSN	15723887
Issue Number	4
Volume Number	34
e-ISSN	15734943
Journal	The Protein Journal
Language	English
Publisher	Springer
Publisher Date	2015-08-01
Publisher Place	Netherlands
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Bacterial Proteins Chemistry Lipase Acrylamide Bacillales Enzymology Circular Dichroism Hydrogen-ion Concentration Protein Structure, Secondary Recombinant Proteins Spectrometry, Fluorescence Journal Article
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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The Effect of pH on Globular State of Lipase-3646; an Appropriate Model for Molten Globule Investigations

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