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| ZHANG,Qiang; WU,Caie; FAN,Gongjian; LI,Tingting; WEN,Xia. |
| Abstract Morchella esculenta (L) Pers. is a highly valued edible and medicinal fungus that remains underutilized. For this study, the effects of glycation treatment on antioxidant activity and characteristics of the M. esculenta protein isolate (MPI) were investigated via the Maillard reaction. Conjugation between MPI and xylose was proven via UV-vis, FT-IR, intrinsic fluorescence analysis, and SDS-PAGE. Amino acid analysis revealed involvement of lysine, arginine and tyrosine in MPI, forming a covalent cross-link with xylose. Differential scanning calorimetry (DSC) results showed that glycated MPI (MPIG) possesses a more favorable thermal stability compared to native MPI (MPIN), heated MPI (MPIH) and an unheated mixture of MPI and xylose (MPI-XM). MPIG... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Maillard reaction; Morchella esculenta protein; Xylose; Thermal stability; Antioxidant activity. |
| Ano: 2018 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612018000100126 |
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| HE,Dongliang; ZHANG,Zhijun; LI,Huizhen; XIA,Yaoyao; LI,Xiaojun; CHEN,Tie. |
| Abstract Response surface methodology (RSM) was used to optimize the ultrasound-assisted extraction parameters of perilla protein isolate (PPI), which has functional properties. A central composite experimental design was applied to investigate the effects of three factors (ultrasonic power, extraction time, and liquid-to-solid ratio) on six responses: protein yield, water solubility index (WSI), water absorption capacity (WAC), oil holding capacity (OHC), emulsifying activity (EA), and foaming ability (FA). Based on the RSM results, the optimum conditions were an ultrasonic power of 206 W, and extraction time of 32.4 min, and a liquid-to-solid ratio of 10.34:1. Under these conditions, PPI had high protein yield (26.1%) and functional properties (55.2%... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Ultrasound-assisted extraction; Perilla protein isolate; Protein yield; Functional properties; Thermal stability; Polypeptide profile. |
| Ano: 2018 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612018000200348 |
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| Moreira,Keila Aparecida; Cavalcanti,Maria Taciana Holanda; Duarte,Helena Simões; Tambourgi,Elias Basile; Melo,Eduardo Henrique Magalhães de; Silva,Valdinete Lins; Porto,Ana Lúcia Figueiredo; Lima Filho,José Luiz de. |
| The partial characterization of extracellular proteases from Streptomyces clavuligerus NRRL 3585 and 644 mutant was investigated. The enzyme production was carried out in batch fermentation using soy bean filtrate as nitrogen source. Maximum activity was obtained after 96h of fermentation with an initial pH of 7.0. The enzyme was partially purified by ammonium sulphate precipitation. Enzymes from the two strains retained 37% of their initial activities at pH 8.0 after 2 h incubation at 25ºC. Enzyme half-life at pH 8.0 and 60ºC was 40.30 and 53.32 min, respectively for both strains (partially purified extract). The optimum pH was obtained at pH 7.0-8.0 and 8.4 for enzymes produced for 3585 and 644 strains (crude extract), respectively, and 8.4 and 8.0 for... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Streptomyces clavuligerus; Extracellular proteases; Thermal stability; PH. |
| Ano: 2001 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822001000300010 |
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| Sudério,Fabrício Bonfim; Barbosa,Gislainy Karla da Costa; Gomes-Filho,Enéas; Enéas-Filho,Joaquim. |
| Three β-galactosidase isoforms, β-gal I and β-gal II (cytosolic) and β-gal III (cell wall-associated), were isolated from stems of Vigna unguiculata (L.) Walp. cv. Pitiúba seedlings. Purification consisted of aμMonia sulfate fractionation followed by chromatography in DEAE-Sephadex and Lactosyl-Sepharose columns. The two cytosolic isoforms showed the same chromatography pattern, which differed from that of β-gal III. Electrophoresis revealed a single band of protein for β-gal II and β-gal III which also expressed β-galactosidase activity in gel. The apparent molecular mass of the β-gal I, II and III was 89, 146 and 124 kDa, respectively. The three isoforms revealed the same optimal pH (4.0) and the same optimal assay temperature (55ºC) for enzyme activity.... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Enzymatic kinetics; Cowpea; Optimal pH; Enzyme purification; Thermal stability; Thermal inactivation. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202011000100003 |
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