PRODUCTION OF CELLULASE AND BETA-GLUCOSIDASE ACTIVITIES FOLLOWING GROWTH OF STREPTOMYCES-HYGROSCOPICUS ON CELLULOSE-CONTAINING MEDIA

L SPEAR; J GALLAGHER; L MCHALE; Anthony McHale

doi:10.1007/BF00130309

PRODUCTION OF CELLULASE AND BETA-GLUCOSIDASE ACTIVITIES FOLLOWING GROWTH OF STREPTOMYCES-HYGROSCOPICUS ON CELLULOSE-CONTAINING MEDIA

L SPEAR, J GALLAGHER, L MCHALE, Anthony McHale

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

16 Citations (Scopus)

Abstract

The actinomycete, Streptomyces hygroscopicus was shown Lo be capable of producing extracellular cellulase and cell associated beta-glucosidase activity during growth on cellulose containing media. Cell homogenates were shown to contain a beta-glucosidase fraction which was stable for up to 24h. at 30-degrees-C and had half-lives of 480min. and 220 min. at 40 and 50-degrees-C, respectively. The enzyme fraction was also shown to be optimally active at pH 4.0 suggesting that it might represent a suitable supplement for fungal cellulase systems, deficient in beta-glucosidase activity.

Original language	English
Pages (from-to)	1265-1268
Journal	Biotechnology Letters
Volume	15
Issue number	12
DOIs	https://doi.org/10.1007/BF00130309
Publication status	Published (in print/issue) - Dec 1993

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@article{70563101e6d3488a9b2292f6c379691c,

title = "PRODUCTION OF CELLULASE AND BETA-GLUCOSIDASE ACTIVITIES FOLLOWING GROWTH OF STREPTOMYCES-HYGROSCOPICUS ON CELLULOSE-CONTAINING MEDIA",

abstract = "The actinomycete, Streptomyces hygroscopicus was shown Lo be capable of producing extracellular cellulase and cell associated beta-glucosidase activity during growth on cellulose containing media. Cell homogenates were shown to contain a beta-glucosidase fraction which was stable for up to 24h. at 30-degrees-C and had half-lives of 480min. and 220 min. at 40 and 50-degrees-C, respectively. The enzyme fraction was also shown to be optimally active at pH 4.0 suggesting that it might represent a suitable supplement for fungal cellulase systems, deficient in beta-glucosidase activity.",

author = "L SPEAR and J GALLAGHER and L MCHALE and Anthony McHale",

year = "1993",

month = dec,

doi = "10.1007/BF00130309",

language = "English",

volume = "15",

pages = "1265--1268",

journal = "Biotechnology Letters",

issn = "1573-6776",

publisher = "Springer",

number = "12",

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T1 - PRODUCTION OF CELLULASE AND BETA-GLUCOSIDASE ACTIVITIES FOLLOWING GROWTH OF STREPTOMYCES-HYGROSCOPICUS ON CELLULOSE-CONTAINING MEDIA

AU - SPEAR, L

AU - GALLAGHER, J

AU - MCHALE, L

AU - McHale, Anthony

PY - 1993/12

Y1 - 1993/12

N2 - The actinomycete, Streptomyces hygroscopicus was shown Lo be capable of producing extracellular cellulase and cell associated beta-glucosidase activity during growth on cellulose containing media. Cell homogenates were shown to contain a beta-glucosidase fraction which was stable for up to 24h. at 30-degrees-C and had half-lives of 480min. and 220 min. at 40 and 50-degrees-C, respectively. The enzyme fraction was also shown to be optimally active at pH 4.0 suggesting that it might represent a suitable supplement for fungal cellulase systems, deficient in beta-glucosidase activity.

AB - The actinomycete, Streptomyces hygroscopicus was shown Lo be capable of producing extracellular cellulase and cell associated beta-glucosidase activity during growth on cellulose containing media. Cell homogenates were shown to contain a beta-glucosidase fraction which was stable for up to 24h. at 30-degrees-C and had half-lives of 480min. and 220 min. at 40 and 50-degrees-C, respectively. The enzyme fraction was also shown to be optimally active at pH 4.0 suggesting that it might represent a suitable supplement for fungal cellulase systems, deficient in beta-glucosidase activity.

U2 - 10.1007/BF00130309

DO - 10.1007/BF00130309

M3 - Article

SN - 1573-6776

VL - 15

SP - 1265

EP - 1268

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 12

ER -

PRODUCTION OF CELLULASE AND BETA-GLUCOSIDASE ACTIVITIES FOLLOWING GROWTH OF STREPTOMYCES-HYGROSCOPICUS ON CELLULOSE-CONTAINING MEDIA

Abstract

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