Examining structure-activity correlations of some high activity enzyme preparations for low water media

Kusum Solanki, Peter J. Halling, Munishwar N. Gupta

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

A first study of the comparison of structures of enzymes (by FT-IR and CD) in different high activity (in low water media) preparations is reported. Using chymotrypsin and subtilisin as models, we have studied various factors that distinguish enzyme precipitated and rinsed with propanol (EPRP), crosslinked enzyme aggregates (CLEA), protein coated microcrystals (PCMC) and crosslinked protein coated microcrystals (CLPCMC). The suspensions in organic media were assayed for catalytic activity, and structures were probed by FT-IR and CD measurements. CD studies of enzyme suspensions were possible by using a rotating cell accessory. There was a generally good correlation between higher catalytic activity and retention of native structures. Activity and retention of native structure was always higher if aqueous enzyme solution was added to propanol rather than vice versa in the precipitation step of these preparations. The work identifies factors which may lead to better biocatalyst designs for low water media.
LanguageEnglish
Pages147-151
Number of pages5
JournalBioresource Technology
Volume115
Issue numberJuly
Early online date20 Dec 2011
DOIs
Publication statusPublished - 2012

Fingerprint

Enzyme activity
enzyme activity
Enzymes
enzyme
Water
Microcrystals
Propanol
1-Propanol
Catalyst activity
water
Suspensions
Proteins
Biocatalysts
protein
Accessories
Subtilisin
Chymotrypsin

Keywords

  • alpha-chymotrypsin
  • subtilisin
  • FT-IR
  • enzymes
  • low water media

Cite this

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Examining structure-activity correlations of some high activity enzyme preparations for low water media. / Solanki, Kusum; Halling, Peter J.; Gupta, Munishwar N.

In: Bioresource Technology, Vol. 115, No. July, 2012, p. 147-151.

Research output: Contribution to journalArticle

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