대두 ${\alpha}-galactosidase$의 정제 및 성질

금종화,오만진,김성렬,Keum, Jong-Hwa,Oh, Man-Jin,Kim, Seong-Yeol 한국응용생명화학회 1991 Applied Biological Chemistry (Appl Biol Chem) Vol.34 No.3

To elucidate enzymatic properties of ${\alpha}-galactosidase$ (EC 3, 2, 1, 22) from germinated soybean, changes in the enzyme activities and oligosaccharide contents during germination of soybean were determined. ${\alpha}-Galactosidase$ from germinated soybean was purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. Their chemical and enzymatic properties was investigated. ${\alpha}-galactosidase$ activity of sobeam was maximized when it was germinated at $25^{\circ}C$ for 120 hour. Raffinose and stachyose in soybean were decomposed completely after 96 hours and 120 hours of germination, respectively. Soybean ${\alpha}-galactosidase$ was purified by 6.6 fold by ammonium sulfate fractionation, ion exchange chromatography on DEAE-Cellulose and Sephadex A-50, and gel filtration on Sephadex G-150. Its specific activity was 825 Units/mg protein and the yield was 2.5% of the total activity of crude extracts. The purified ${\alpha}-galactosidase$ of soybean was found to be homogeneous by polyacrylamide gel electrophoresis and by HPLC. Isoelectric point of soybean ${\alpha}-galactosidase$ was determined analytical isoelectric focusing to be pH 4.8. The soybean ${\alpha}-galactosidase$ was monomeric and its molecular weight was estimated to be 30,000 by SDS-PAGE. The optimal temperature and pH for the soybeam ${\alpha}-galactosidase$ activity were $40^{\circ}C$ and pH 6.0 and 75% of its activity was lost by heating at $60^{\circ}C$ for 10 min. The enzyme was appeared to have higher affinity to raffinose than to stachyose. The Km value of soybean enzyme was 5.3 mM for ${\rho}-nitrophenyl-{\alpha}-D-galactopyranoside$ and the activation energy on PNPG was calculated to be 13.02 Kcal per mole. 대두 발아 과정 중의 ${\alpha}-galactosidase$를 추출하여 염석, 이온교환 크로마토그래피 및 겔 여과 등의 방법으로 정제한 후 정제효소의 효소학적 성질을 검토하였다. 대두 ${\alpha}-galactosidase$의 활성은 $25^{\circ}C$에서 120시간 발아시켰을 때 가장 높았으며, 대두 중의 raffinose는 96시간, stachyose는 120시간 발아시켰을 때 완전히 분해되었다. 대두 ${\alpha}-galactosidase$는 황산암모늄염석, DEAE-Cellulose 및 DEAE-Sephadex A-50 이온교환 크로마토그래피, Sephadex G-150 겔 여과 등에 의하여 비활성은 825U/mg protein으로써 6.6배까지 정제되었으며 수율은 2.5%이었고 HPLC와 PAGE에 의하여 순도를 확인하였다. 정제효소의 등전점은 pH 4.8이었고, 분자량은 30,000인 monomer이었으며 정제효소의 최적작용 PH는 6.0, 최적작용온도는 $40^{\circ}C$ 이었고, $60^{\circ}C$에서 10분 처리시 25%의 잔존 활성을 나타내었다. 정제효소는 stachyose보다 raffinose를 쉽게 분해하였으며 PNPG에 대한 Km값은 5.3 mM, 활성화 에너지는 13.02 cal/mole이었다.

${\alpha}-Galactosidase$의 활력차이에 의한 Bifidobacteria의 선별

민해기,이시경,강국희,Min, Hae-Ki,Lee, See-Kyung,Kang, Kook-Hee 한국응용생명화학회 1993 Applied Biological Chemistry (Appl Biol Chem) Vol.36 No.3

본 연구는 합성기질인 $X-{\alpha}-Gal$를 이용하여 발효유 및 유제품내의 Bifidobacteria 생균수를 측정할 목적으로 하였다. 젖산균과 Bifidobacteria의 ${\alpha}-galactosidase$ specific activity를 측정한 결과 Bifidobacteria 균주에서는 높은 ${\alpha}-galactosidase$ activity를 가지고 있었으며, 그 중 Bif. longum KCTC 3215의 specific activity는 8.57 unit/mg protein으로 가장 높게 나타났다. Lactobacillus, Streptococcus, Pediococcus와 Leuconostoc 균주에서는 활성이 미약하거나 없었다. 합성기질인 $X-{\alpha}-Gal$을 MRS agar 배지에 $100{\;}{\mu}M$ 첨가한 결과 Bifidobacteria는 blue colony로, Lac. bulgaricus, Lac. casei와 Leu. mescenteroides 균주는 light blue colony로, 그 외 젖산균에서는 white colony로 나타났다. This method using the synthesis substrate of $5-bromo-4-chloro-3-indolyl-{\alpha}-galactoside\;(X-{\alpha}-Gal)$ was examined for the differential enumeration of Bifidobacteria and lactic acid-producing bacteria. Bifidobacteria possess a high level of ${\alpha}-galactosidase$ activity. Bifidobacterium longum KCTC 3215 exhibited the highest ${\alpha}-galactosidase$ specific activity (8.57 units/mg protein). Determination of ${\alpha}-galactosidase$ activity using the PNPG procedure showed that Lactobacillus, Streptococcus, Pediococcus, and Leuconostoc strain had lower ${\alpha}-galactosidase$ activity as compared to Bifidobacteria. The $X-{\alpha}-Gal$ based medium is useful to identify Bifidobacteria among lactic acid-producing bacteria since the enzyme action of ${\alpha}-galactosidase$ spills $X-{\alpha}-Gal$ substrate and releases indol which impacts a blue color to Bifidobacterial colonies on agar plates. All strains of Bifidobacteria appeared as blue colonies on MRS agar medium supplemented with $100\;{\mu}M\;X-{\alpha}-Gal$ while colonies of other lactic acid-producing bacteria appeared white or light blue.

Removal of Alpha-Gal Epitopes from Porcine Aortic Valve and Pericardium using Recombinant Human Alpha Galactosidase A

Park, Seongsik,Kim, Woong-Han,Choi, Sun-Young,Kim, Yong-Jin The Korean Academy of Medical Sciences 2009 JOURNAL OF KOREAN MEDICAL SCIENCE Vol.24 No.6

<P>It has been reported that the immune response due to α-Gal epitopes is an important factor in tissue valve failure. The elimination of the interaction between the natural anti-Gal antibodies and α-gal epitopes on the xenografts is a prerequisite to the success of xenografts in humans. Previously, we reported that the green coffee bean α-galactosidase could remove all α-Gal epitopes from cell surface of porcine aortic valve and pericardial tissue, but it has limitations on cost effectiveness. In this study we wanted to know whether the recently produced recombinant human α-galactosidase A has the same effective enzymatic activity as green coffee bean α-galactosidase in removing α-Gal epitopes from the same tissues. After treating fresh porcine aortic valve and pericardial tissue with recombinant α-galactosidase A, each sample was stained with <I>Griffonia simplicifolia</I> type I isolectin B4 indirect immunoperoxidase avidin-biotin technique. We then examined whether the α-Gal epitopes were reduced or abolished in each consecutive concentration of recombinant α-galactosidase A by comparing the degree of the <I>Griffonia simplicifolia</I> isolectin B4 staining. As a result, the recombinant α-galactosidase A could remove cell surface α-Gals on porcine aortic valve and pericardial tissue as effectively as green coffee bean α-galactosidase.</P>

균체외 \alpha-galactosidase를 생산하는 Streptomyces sp. YB-4의 분리 및 효소 특성

김소영,조기행,김창진,박동진,윤기홍 한국미생물 · 생명공학회 2002 한국미생물·생명공학회지 Vol.30 No.4

토양으로부터 세포외로 $\alpha$-galactosidase를 분비 생산하는 방선균 YB-4가 분리되었으며, 분리균의 배양ㆍ형태ㆍ생리적 특성을 조사한 결과 Streptomyces 속 균주로 확인되었다. 분리균의 배양상등액으로부터 부분정제된 $\alpha$-galactosidase를 조효소액으로 사용하였을 때 para-nitrophenyl-$\alpha$-D-galacto-pyranoside는 pH 6.0과 6$0^{\circ}C$의 반응조건에서 가장 잘 분해되었으며, 조효소액을 pH 4.0에서 pH 10.0범위에서 1시간 이상 방치한 후에도 약 90% 이상의 $\alpha$-galactosidase 활성을 유지하였다. 또한 분리균이 생산하는 $\alpha$-galactosidase는 melibiose, raffinose와 stachyose와 같은 저당류를 가수분해 할 수 있으며 분해산물로 galactose를 방출하는 것으로 보아 $\alpha$-1,6 결합을 분해한 것으로 확인되었다. A strain YB-4 producing the extracellular $\alpha$-galactosidase was isolated from soil, and has been identified as Streptomyces sp. on the basis of its cultural, morphological and physiological properties. The partially purified $\alpha$-galactosidase was most active on paranitrophenyl-$\alpha$-D-galactopyranoside at pH 6.0 and 6$0^{\circ}C$. The enzyme retained 90% of its maximum activity between pH 4.0 and pH 10.0 after pre-incubation for 1 h. The enzyme was able to hydrolyze oligomeric substrates such as melibiose, raffinose and stachyose to liberate galactose residue, indicating that the $\alpha$-galactosidase of Steptomyces sp. YB-4 hydrolyzed $\alpha$-1,6 linkage.

Aspergillus niger $\alpha$-Galactosidase의 정제 및 성질

금종화,오만진,김찬조 한국미생물 · 생명공학회 1991 한국미생물·생명공학회지 Vol.19 No.5

Aspergillus niger가 생산하는 $\alpha$-galactosidase의 효소학적 성질을 조사하기 위하여 시험균주를 밀기울 배양한 후 생성된 $\alpha$-galactosidase를 염석, 이온교환 크로마토그래피 및 겔 여과 등의 방법으로 정제한 후 정제효소의 효소학적 성질을 검토하였다. Asp. niger를 밀기울 배지에서 $30^{\circ}C$, 4일 배양했을 때 효소활성이 가장 높았으며 $\alpha$-galactosidase는 황산암모늄 염석, DEAE-cellulose 및 DEAE-Sephadex A-50 이온교환 크로마토그래피, sephadex G-150 겔 여과 등에 의하여 23.7배까지 정제되었으며 비활성이 1,229U/mg.protein, 수율 14이었고 HPLC와 PAGE에 의해 순도가 확인되었다. To elucidate enzymatic properties of a-glactosidase (EC 3.2.1.22) from Asp. niger, a-galactosidase from wheat bran culture was purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. And then its enzymatic propeties were investigated. The highest level of $\alpha$-galactosidase activity was obtained when Asp. niger was grown on wheat bran medium at $30^{\circ}C$ for 96 hours. The $\alpha$-galactosidase was purified by 23.7 fold by ammonium sulfate fractionation, ion exchange chromatography on DEAE-Celluose and Sephadex A-50, and gel filtration on Sephadex G-150 and its specific activity was 1,229 Unitslmg protein and the yield was 14% of the total activity of wheat bran culture. The purified $\alpha$-galactosidase was found to be homogeneous by polyacrylamide gel electrophoresis and HPLC. The $\alpha$-galactosidase was a tetrameric glycoprotein which consisted of identical subunits with molelcular weight of 28,000 each by SDS-PAGE and isoelectric point was determined analytical isoelectric focusing to be pH 4.6. The optimal temperature and pH for the $\alpha$-galactosidase activity were $40^{\circ}C$ and pH 6.5, respectively, and 54% of its activity was lost by heating at $60^{\circ}C$ for 10 mins, It was appeared to have higher affinty to raffinose than to stachyose. The K, value and activation energy of $\alpha$-galactosidase were 5.0 mM and 8.515 Kcal per mole for p-nitrophenyl- $\alpha$--D-galactopyranoside, respectively.

Weissella cibaria가 생산하는${\alpha}$-Galactosidase 및 ${\beta}$-Glucosidase의 특성

홍성욱,류래균,정병문,김완식,정건섭,Hong, Sung-Wook,You, Lae-Kyun,Jung, Byung-Moon,Kim, Wan-Sik,Chung, Kun-Sub 한국미생물·생명공학회 2009 한국미생물·생명공학회지 Vol.24 No.3

대두의 발효를 통하여 생리활성을 가지고 있는 이소플라본 aglycone 함량을 높이기 위한 ${\beta}$-glucosidase와 대두에 다량 함유되어 있는 stachyose, rafinose와 같은 난소화성 oligosaccharides를 분해하기 위해 ${\alpha}$-galactosidase 효소 분비 미생물을 김치로부터 ${\alpha}$-galactosidase와 ${\beta}$-glucosidase를 생산하는 미생물을 탐색하였다. 탐색과정을 위해서 선별한 미생물을 16S rDNA sequencing 동정한 결과, Weissella cibaria 동정되어 Weissella cibaria K-M1-4로 명명하였다. Weissella cibaria K-Ml-4를 대두 액체배지에서 18시간동안 배양한 후, 생산한 효소는 배양액을 에탄을 침전, DEAE sepharose, sephacryl S-100HR column chromatography 통하여 ${\alpha}$-galactosidase의 경우, 정제도 5.3배, 수율 3.5% 그리고 ${\beta}$-glucosidase의 경우, 정제도 4.4배, 수율 2.9%로 정제되었다. ${\alpha}$-Galactosidase 효소특성은 $60^{\circ}C$에서 최대 활성을 나타내었으며, $80^{\circ}C$에서 30분 처리시 43% 잔존활성을 보였다. pH 8.0에서 최대 활성을 나타내었으며, pH 5.0-9.0에서 안정하였다. 금속이온에 대한 영향에서 $Fe^{2+}$과 $Cu^{2+}$을 첨가하였을 때 효소 활성이 증가하였다. p-Nitrophenyl-${\alpha}$-D-galacto-pyranoside (PNPG) 기질에 대한 Km은 0.98 mM이었고, Vmax는 $1.81{\mu}$mole/min 이었다. ${\beta}$-Glucosidase 효소 특성은 $50^{\circ}C$에서 최대 활성을 나타내었으며, $80^{\circ}C$에서 30분 처리시 46% 잔존활성을 보였다. pH 7.0에서 최대 활성을 나타내었으며, pH 5.0-9.0에서 안정하였다. 금속이온에 대한 영향에서 $Fe^{2+},\;Co^{2+},\;Cu^{2+}$을 첨가하였을 때 효소 활성이 증가하였다. p-Nitrophenyl-${\beta}$-D-gluco-pyranoside (PNPG)에 대한 Km값은 1.24mM이었고, Vmax는 $6.81{\mu}$mole/min 이었다. A strain producing ${\alpha}$-galactosidase and ${\beta}$-glucosidase was isolated from Kimchi. The isolated strain was identified as Weissella cibaria by 16S rDNA analysis and designated as Weissella cibaria K-M1-4. The enzyme activity of ${\alpha}$-galactosidase and ${\beta}$-glucosidase reached the maximum in the soy medium at $37^{\circ}C$ for 24 hr. The enzymes were purified by ethanol fractionation, DEAE sepharose fast flow, and sephacryl S-100HR column chromatography. ${\alpha}$-Galactosidase specific activity was shown by 576 Units/mg protein and the yield was 3.5% of the total activity of crude extracts. ${\beta}$-glucosidase specific activity was shown by 480 Units/mg protein and the yield was 2.9% of the total activity of crude extracts. The optimum temperature for ${\alpha}$-galactosidase was $60^{\circ}C$ and 43% of its original activity remained when it was treated at $80^{\circ}C$ for 30 min. For ${\alpha}$-galactosidase shows the optimum pH of 8.0 and is fairly stable between pH5.0 and pH9.0. The enzyme activity was increased in the presence of $Fe^{2+}$ and $Cu^{2+}$. The value of Km and Vmax for the enzyme were 0.98 mM and $1.81{\mu}$mole/min, respectively. The ${\beta}$-glucosidase has the optimum temperature of $50^{\circ}C$ and 46% of its original activity remained when it was treated at $80^{\circ}C$ for 30min. Its optimum pH of 7.0 and is fairly stable between pH5.0 and pH9.0. The enzyme activity was increased in the presence of $Fe^{2+},\;Co^{2+}$ and $Cu^{2+}$. The value of Km and Vmax for the enzyme were 1.24 mM and $6.81{\mu}$mole/min, respectively.

Mortierella sp. 유래 ${\alpha}$-Galactosidase의 기질특이성

박귀근,Park, Gwi-Gun 한국미생물·생명공학회 2011 한국미생물·생명공학회지 Vol.39 No.3

Mortierella sp. 유래 효소 정제는 CM-sephadex C-50 column chromatography와 Sephadex G-100 column에 의해 수행하여 SDS-전기영동에서 단일밴드를 확인하였고 분자량은 57kDa로 결정되었다. melibiose, raffinose 및 stachyose의 세 종류의 기질에 대한 특이성에서는 Mortierella sp. 유래 정제 ${\alpha}$-galactosidase는 세 종류 기질의 비환원말단에 위치하고 있는 galactose를 모두 유리하는 특이성이 있음을 확인하였다. Bacillus sp. 유래의 $Gal^3Man_4$에 대해서 반응초기 3시간부터 가수분해가 진행되어 반응말기에서는 galactose, mannotetraose 그리고 분해되지 않고 일부 남아있는 $Gal^3Man_4$의 spot이 출현된 반면, 중합도 7의 $Gal^{2,3}Man_5$에 대해서는 반응초기부터 말기까지 전혀 특이성이 없음을 시사하였다. Trichoderma harzianum 유래의 $Gal^2Man_3$에 대해서는 반응초기 3시간부터 가수분해가 진행되어 일부 galactose와 mannotriose spot이 출현되고 있는 반면, 중합도 7의 $Gal^2Man_6$에 대해서는 Bacillus sp. 유래의 중합도 7의 $Gal^{2,3}Man_5$와 동일하게 galactose를 절단하는 능력이 없는 특이성을 보이고 있다. Xylogone sphaerospora 유래의 $Gal^2Man_3$는 Trichoderma harzianum 유래의 중합도 4와 동일한 구조로서 가수분해 시간 경과에 따른 반응말기에서 역시 galactose, mannotriose 및 잔존하는 $Gal^2Man_3$ spot이 출현하고 있는 반면 중합도 6인 $Gal^2Man_5$에 대해서는 mannopentaose의 환원말단부터 2번 mannose에 결합하고 있는 galactose에 대해서는 역시 특이성을 나타내지 않아 반응 초기부터 말기까지 가수분해 pattern에 대한 변화를 보이지 않고 있다. [ ${\alpha}$ ]Galactosidase was purified from a culture filtrate of Mortierella sp. by CM-sephadex C-50, and subsequent Sephadex G-100 column chromatography. The final preparation thus obtained showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight was determined to be 56 kDa. $Gal^3Man^4$ ($6^3$-mono-O-${\alpha}$-D-galactopyranosyl-4-O-${\beta}$-D-mannotetraose), $Gal^{2,3}Man_5$ ($6^{2,3}$-di-O-${\alpha}$-D-galactopyranosyl-4-O-${\beta}$-D-mannopentaose), $Gal_2Man_3$ ($6^2$-mono-O-${\alpha}$-D-galactopyranosyl-4-O-${\beta}$-D-mannotriose), $Gal^2Man_6$ ($6^2$-mono-O-${\alpha}$-D-galactopyranosyl-4-O-${\beta}$-D-mannohexaose) and $Gal^2Man_5$ ($6^2$-mono-O-${\alpha}$-D-galactopyranosyl-4-O-${\beta}$-D-mannopentaose), prepared from 3 types of microbial ${\beta}$-mannnanase, were used as substrates. $Gal^3Man_4$ and $Gal^2Man_3$ had a stubbed ${\alpha}$-galactosyl residue on the $2^{nd}$ and $3^{rd}$ mannose from the reducing end of mannotetraose and mannotriose, thus ${\alpha}$-galactosidase showed a preference for stubbed ${\alpha}$-galactosyl residue. ${\alpha}$-Galactosidase hydrolyzed $Gal^3Man_4$ more rapidly than $Gal^2Man_3$. However, ${\alpha}$-galactosidase hardly acted on $Gal^{2,3}Man_5$, $Gal^2Man_6$ or $Gal^2Man_5$. The enzyme hydrolyzed melibiose to galactose and glucose, raffinose to galactose and sucrose, and also stachyose to galactose and raffinose.

$\alpha$-Galactosidase를 생산하는 Bacillus lichennformis YB-42의 분리와 효소 특성

김현숙,이경섭,소재호,이미성,최준호,윤기홍 한국미생물·생명공학회 2004 한국미생물·생명공학회지 Vol.32 No.2

가정에서 제조된 된장으로부터 -galactosidase의 생산균으로 분리된 YB-42는 형태적 특성, 생화학적 성질 및 16S rRNA의 염기서열에 근거하여 Bacillus licheniformis로 동정되었다. B. lichentyormiE YB-42의 -galactosidase 활성은 균체내ㆍ외에서 모두 관찰되었다. 배양상등액으로부터 DEAE-Sepharose와 Q-Sepharose 컬럼 크로마토그래피를 통해 부분 정제한 -galactosidase을 사용하여 para-nitrophenyl--D-galactopyranoside(pNP-Gal)의 가수분해 반응특성을 조사한 결과 와 pH 6.5에 서 최대 활성을 보였다. Melibiose, raffinose와 stachyose는 부분 정제효소액에 의해 완전히 가수분해 되었으며, 분해산물로 galactose가 생성된 것으로 보아 -1,6 결합이 분해된다는 것이 확인되었다. 한편 pNP-Gal과 melibiose의 가수분해 활성은 galactose에 의해 가장 크게 저해되었으며, galactose보다는 낮지만 pNP-Gal의 가수분해 활성이 mannose와 glucose에 의해서도 저해되는 것으로 나타났다. A bacterium producing the $\alpha$-galactosidase was isolated from Korean soybean paste. The isolate YB-42 has been identified as Bacillus licheniformis on the basis on its 16S rRNA sequence, morphology and biochemical properties. The $\alpha$-galactosidase activity was detected in both the culture supernatant and the cell extract of B. licheniformis YB-42. The partially purified extracellular $\alpha$-galactosidase was obtained from the culture supernatant by DEAE-Sepharose column and Q-Sepharose column chromatography. The enzyme showed the maximum activity for hydrolysis of para-nitrophenyl-$\alpha$-D-galactopyranoside (pNP-$\alpha$Gal) at pH 6.5 and $45^{\circ}C$. It was able to hydrolyze oligomeric substrates such as melibiose, raffmose and stachyose to liberate galactose residue, indicating that the a-galactosidase of B. licheniformis YB-42 hydrolyzed $\alpha$-1,6 linkage. The hydrolyzing activity of $\alpha$-galactosidase for both pNP-$\alpha$Gal and melibiose was dramatically decreased by galactose. Both glucose and mannose inhibited the activity for pNP-$\alpha$Gal less than galactose.

Purification and Characterization of an α-D-Galactosidase from Grape Berry

Kang, Han-Chul,Kim, Tae-Su 한국응용생명화학회 2000 Journal of Applied Biological Chemistry (J. Appl. Vol.43 No.3

Glycosidase activities were tested from the grape berries, Vitis labruscana B. Takasumi. Among various glycosidases, $\alpha$-D-galactosidase was found to be the most active in the flesh and other glycosidases were considerably active in the order of the following: $\alpha$-D-mannosidase>$\alpha$-D-glucosidase>$\beta$-D-glucosidase>$\beta$-D-galactosidase. In the seeds, $\alpha$-D-glucosidase activity was the highest and other glycosidases such as $\alpha$-D-galactosidase, $\beta$-D-glucosidase, and $\beta$-D-galactosidase were still significantly active. The $\alpha$-D-galactosidase in the grape flesh was purified over 83-folds through salting-out with $(NH_4)_2SO_4$ and a series of chromatographies employing Sephadex G-50, Octyl-Sepharose, Q-Sepha- rose, and Biogel P-100. The enzyme was a monomer of 45 kDs as determined through SDS-PAGE and Sephacryl S-200 chromatography. The purified enzyme showed a preference of $\alpha$-D-galactose to $\beta$-D-galactose as a substrate about 5.4 times. Sulfhydryl specific reagents such as N-ethylmaleimide and iodoacetamide significantly inhibited the enzyme activity to the extents of 48 and 52% of its initial activity, respectively. The optimumpH range of $\alpha$-D-galactosidase was around 6.5-7.0. The enzyme activity increased by 46% in the presence of 1mM $Fe^{2+}$.

Effects of α-Galactosidase Supplementation on Performance and Energy Metabolism for Broilers Fed Corn-non-dehulled Soybean Meal Diets

Zhang, Bo,Cao, Yunhe,Chen, Yiqun,Li, Yihang,Qiao, Shiyan,Ma, Yongxi Asian Australasian Association of Animal Productio 2010 Animal Bioscience Vol.23 No.10

To study the effects of ${\alpha}$-galactosidase (${\alpha}$-Gal) supplementation on performance and energy metabolism, 216 Arbor Acres male broilers were placed in 36 cages of 6 birds each and allotted to 4 diets for 42 d, with 0-21 d as starter period and 22-42 d as grower period. The 4 diets were based on corn non-dehulled soybean meal in a $2{\times}2$ factorial arrangement, with 2 levels of ${\alpha}$-Gal (0 vs. 60 U/kg feed) and 2 levels of ME (normal metabolizable energy (NME) and low metabolizable energy (LME)). Bird performance was obtained at 21 and 42 d of age with samples of feces collected for nutrient digestibility from 19-21 d and 40-42 d. At 21 and 42 d, 1 bird from 6 cages of each treatment was killed to determine liver weight, intestinal pH and chyme viscosity. With the addition of ${\alpha}$-Gal the 42 d body weight (BW) and 0-42 d average daily gain (ADG) were significantly improved (p<0.05). Average daily feed intake (ADFI) of birds fed the LME diet was significantly increased compared to those fed the NME diet during starter (p<0.01) and grower (p<0.05) periods and overall (p<0.01). There was an interaction of ${\alpha}-Gal{\times}ME$ on 0-21 d ADFI (p<0.01). Supplementation of ${\alpha}$-Gal significantly improved (p<0.01) feed efficiency during the grower period and overall. Feed efficiency of birds fed the LME diet was significantly decreased (p<0.05) compared to those fed the NME diet during the starter period and overall. With the addition of ${\alpha}$-Gal apparent metabolizable energy (AME) was improved (p<0.01) by 2.1% and 1.8% during starter and grower periods, respectively. There was a main effect (p<0.05) of ${\alpha}$-Gal on the digestion of neutral detergent fiber (NDF) during the starter period and crude protein (CP), NDF and acid detergent fiber (ADF) during the grower period. With the addition of ${\alpha}$-Gal, the relative weight of liver was reduced (p<0.01) during the two phases. The duodenal and jejunal pH were significantly decreased (p<0.01) with the supplementation of ${\alpha}$at the two phases. ${\alpha}$-Gal addition reduced (p<0.01) chyme viscosity of the ileum during the starter and grower periods. Overall, ${\alpha}$-Gal showed a major effect on nutrient efficiency, improved ADG and feed efficiency, whereas LME decreased feed efficiency. The incorporation of ${\alpha}$-Gal into a LME diet could at least partially offset ME deficiency of non-dehulled soybean meal.