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

Access to Document

10.1271/bbb.61.893

Fingerprint Dive into the research topics of 'Preparation of glutaraldehyde cross-linked complex from support'. Together they form a unique fingerprint.

Cite this

@article{46edd1c8a2a1424b9a70b2a0a200d5d2,

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",

month = jan,

doi = "10.1271/bbb.61.893",

language = "English",

volume = "61",

pages = "893--895",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "5",

}

TY - JOUR

T1 - Preparation of glutaraldehyde cross-linked complex from support

AU - Matsui, Toshiro

AU - Oki, Tomoyuki

AU - Matsumoto, Kiyoshi

AU - Osajima, Yutaka

PY - 1997/1

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.

UR - http://www.scopus.com/inward/record.url?scp=0030800249&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030800249&partnerID=8YFLogxK

U2 - 10.1271/bbb.61.893

DO - 10.1271/bbb.61.893

M3 - Article

AN - SCOPUS:0030800249

VL - 61

SP - 893

EP - 895

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

SN - 0916-8451

IS - 5

ER -