Preparation of glutaraldehyde cross-linked complex from support

Toshiro Matsui; Tomoyuki Oki; Kiyoshi Matsumoto; Yutaka Osajima

doi:10.1271/bbb.61.893

Preparation of glutaraldehyde cross-linked complex from support

Toshiro Matsui, Tomoyuki Oki, Kiyoshi Matsumoto, Yutaka Osajima

Food Science and Biotechnology

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

A glutaraldehyde (GA) spacer complex on enzyme immobilization was cleaved from the support introduced N^α -9-fluorenylmethyl-oxycarbonylglycine. By the ¹H-NMR spectroscopic measurement of the desired complex, glycine-GA-phenethylamine (GGP), GA was thought to be involved in enzyme immobilization as a heteropolymer with the molecular weight range of about 600 to 1300.

Original language	English
Pages (from-to)	893-895
Number of pages	3
Journal	Bioscience, Biotechnology and Biochemistry
Volume	61
Issue number	5
DOIs	https://doi.org/10.1271/bbb.61.893
Publication status	Published - Jan 1997

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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Cite this

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title = "Preparation of glutaraldehyde cross-linked complex from support",

abstract = "A glutaraldehyde (GA) spacer complex on enzyme immobilization was cleaved from the support introduced Nα -9-fluorenylmethyl-oxycarbonylglycine. By the 1H-NMR spectroscopic measurement of the desired complex, glycine-GA-phenethylamine (GGP), GA was thought to be involved in enzyme immobilization as a heteropolymer with the molecular weight range of about 600 to 1300.",

author = "Toshiro Matsui and Tomoyuki Oki and Kiyoshi Matsumoto and Yutaka Osajima",

year = "1997",

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doi = "10.1271/bbb.61.893",

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AU - Osajima, Yutaka

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Y1 - 1997/1

N2 - A glutaraldehyde (GA) spacer complex on enzyme immobilization was cleaved from the support introduced Nα -9-fluorenylmethyl-oxycarbonylglycine. By the 1H-NMR spectroscopic measurement of the desired complex, glycine-GA-phenethylamine (GGP), GA was thought to be involved in enzyme immobilization as a heteropolymer with the molecular weight range of about 600 to 1300.

AB - A glutaraldehyde (GA) spacer complex on enzyme immobilization was cleaved from the support introduced Nα -9-fluorenylmethyl-oxycarbonylglycine. By the 1H-NMR spectroscopic measurement of the desired complex, glycine-GA-phenethylamine (GGP), GA was thought to be involved in enzyme immobilization as a heteropolymer with the molecular weight range of about 600 to 1300.

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SN - 0916-8451

IS - 5

ER -

Preparation of glutaraldehyde cross-linked complex from support

Abstract

All Science Journal Classification (ASJC) codes

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