Immobilization of spinach leaf hydroperoxide lyase

L. M. Simon, Sz J. Márczy, M. Kotormán, Sz Á Németh, B. Szajáni

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Spinach leaf hydroperoxide lyase (HPLS) was immobilized on polyethylene terephthalate (Sorsilen), silica (Silochrome) and polyacrylamide (Akrilex) supports. The highest immobilized activity (360 mU g1 dry gel) was achieved with the HPLS bound to Akrilex C. The Akrilex and Silochrome-bound enzymes were studied with respect to their thermal, pH and operational stabilities relative to those of the soluble HPLS. The Akrilex-bound enzyme had the highest stability.

Original languageEnglish
Pages (from-to)547-552
Number of pages6
JournalProgress in Biotechnology
Volume15
Issue numberC
DOIs
Publication statusPublished - 1998

Fingerprint

Spinacia oleracea
Immobilization
Silica Gel
Polyethylene Terephthalates
Enzymes
Silicon Dioxide
Hot Temperature
Gels
hydroperoxide lyase

ASJC Scopus subject areas

  • Biotechnology

Cite this

Immobilization of spinach leaf hydroperoxide lyase. / Simon, L. M.; Márczy, Sz J.; Kotormán, M.; Németh, Sz Á; Szajáni, B.

In: Progress in Biotechnology, Vol. 15, No. C, 1998, p. 547-552.

Research output: Contribution to journalArticle

Simon, L. M. ; Márczy, Sz J. ; Kotormán, M. ; Németh, Sz Á ; Szajáni, B. / Immobilization of spinach leaf hydroperoxide lyase. In: Progress in Biotechnology. 1998 ; Vol. 15, No. C. pp. 547-552.
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