ENZYMATIC-HYDROLYSIS OF THE HORN AND HOOF OF COW AND BUFFALO

被引:41
作者
KIDA, K
MORIMURA, S
NODA, J
NISHIDA, Y
IMAI, T
OTAGIRI, M
机构
[1] KUMAMOTO UNIV,FAC PHARMACEUT SCI,KUMAMOTO 862,JAPAN
[2] NISHIDA CO,NARA 63601,JAPAN
来源
JOURNAL OF FERMENTATION AND BIOENGINEERING | 1995年 / 80卷 / 05期
关键词
KERATIN; ENZYMATIC HYDROLYSIS; REPEATED-BATCH REACTION; RECYCLING; LIVESTOCK WASTE;
D O I
10.1016/0922-338X(96)80923-8
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 [微生物学]; 0836 [生物工程]; 090102 [作物遗传育种]; 100705 [微生物与生化药学];
摘要
With the aim of efficiently utilizing livestock waste as a protein resource, we studied their enzymatic hydrolysis. Particles of a mixture of horn and hoof from cow and buffalo with a diameter of less than 250 mu m were selected for use as substrate, and a proteinase from Bacillus subtilis, selected from among various commercial proteolytic enzymes was used. For enzymatic hydrolysis of the substrate, heat treatment was absolutely necessary prior to digestion and the conditions for the enzymatic reaction were determined to be as follows: reaction time, 30 to 60 min; pH, 8.3; temperature, 50 degrees C; weight ratio of substrate to enzyme, 1:0.05; and concentration of substrate, 62.5 g/l. Even when a membrane reactor was used, the amount of enzyme required could not be reduced. However, repeated-batch reaction allowed us to reduce the added amount of enzyme. The enzyme was added only for the first round of the reaction in four rounds of repeated-batch reaction. As a result of this process, the weight ratio of substrate to the enzyme was reduced to 1:0.023 from 1:0.05 at a final substrate concentration of 61 g/l.
引用
收藏
页码:478 / 484
页数:7
相关论文
共 14 条
[1]
PROTEASE PRODUCTION BY A THERMOPHILIC BACILLUS SPECIES (P-001A) WHICH DEGRADES VARIOUS KINDS OF FIBROUS PROTEINS [J].
ATALO, K ;
GASHE, BA .
BIOTECHNOLOGY LETTERS, 1993, 15 (11) :1151-1156
[2]
CHIBA H, 1987, BIOSCI BIOTECHNOL, V25, P396
[3]
FISH WW, 1969, J BIOL CHEM, V244, P4989
[4]
SYNTHESIS OF HUMAN RENIN INHIBITORY PEPTIDES, ANGIOTENSINOGEN TRANSITION-STATE ANALOGS CONTAINING A RETRO-INVERSO AMIDE BOND [J].
HARADA, H ;
IIZUKA, K ;
KAMIJO, T ;
AKAHANE, K ;
YAMAMOTO, R ;
NAKANO, Y ;
TSUBAKI, A ;
KUBOTA, T ;
SHIMAOKA, I ;
UMEYAMA, H ;
KISO, Y .
CHEMICAL & PHARMACEUTICAL BULLETIN, 1990, 38 (11) :3042-3047
[5]
HOSHINO M, 1976, YAKUGAKU, V25, P793
[6]
KIMURA S, 1990, ACTA PHARM NORDICA, V2, P65
[7]
OPIOID ACTIVITIES AND STRUCTURES OF ALPHA-CASEIN-DERIVED EXORPHINS [J].
LOUKAS, S ;
VAROUCHA, D ;
ZIOUDROU, C ;
STREATY, RA ;
KLEE, WA .
BIOCHEMISTRY, 1983, 22 (19) :4567-4573
[8]
CATIONIZATION OF PROTEIN ANTIGENS .6. EFFECTS OF CATIONIZATION ON THE IMMUNOREGULATORY PROPERTIES OF A BOVINE SERUM-ALBUMIN PEPTIDE, A.A. 506-589 [J].
MICHAEL, JG .
CELLULAR IMMUNOLOGY, 1991, 138 (01) :121-129
[9]
INFRARED SPECTRA OF POLYPEPTIDES IN VARIOUS CONFORMATIONS - AMIDE I AND II BANDS [J].
MIYAZAWA, T ;
BLOUT, ER .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1961, 83 (03) :712-&
[10]
MOTIKAWA T, 1984, BIOCHEM BIOPH RES CO, V119, P1205