Qarakhanids on the Edge of the Bukhara Oasis: archaeobotany of Medieval Paykend

The urban center of Paykend was an exchange node just off the main corridor of the Silk Road in the Bukhara Oasis on the edge of the hyperarid Kyzyl–Kum Desert. The city was occupied from the end of 4 century B.C.E. to the mid–12 century C.E.; our study focuses on the Qarakhanid period (C.E. 999 – 1211), the last imperial phase of urban occupation at Paykend before its abandonment. In this study, we present the results of an analysis of archaeobotanical remains recovered from a multifunction rabat, which appears to have comprised a domicile, military structure, center of commerce, and/or a caravanserai, a roadside inn for travelers. We shed light on how people adapted a productive economy to the local ecological constraints. By adding these data to the limited Qarakhanid archaeobotany from across Central Asia, we provide the first glimpses into cultivation, commerce, and consumption at a Silk Road trading town along the King’s Road, the central artery of ancient Eurasia.Introduction Paykend and Its Environment Materials and Methods Results - Radiocarbon Dating - Archaeobotany - Domesticated Crops - Fruits and Nuts - Wild Herbaceous Plants Discussion - Taphonomy - Agriculture in the Hyper–Arid Desert -- Ecological Constraints - Arboriculture and Cash Crops at Paykend Conclusio

The Uzbek-American expedition in Bukhara: preliminary report on the third season (2017)

Excavations at the site of Bashtepa, at the western interface of the Bukhara oasis and the Kyzyl-kum desert, and at the kurgan sites at Kuyu-Mazar and Lyavandak on the eastern and north eastern fringes of the oasis, are detailed here, enriching our understanding of agro-pastoralism in Antiquity. At Bashtepa, results indicate a shifting site function, from a border fortress, over a phase during which a monumental though still poorly understood platform dominated the northern part of the site, to a final phase when the site evolved into a small rural settlement characterized by pit houses. Preliminary archaeo-botanical and paleo-zoological studies demonstrate an engagement with grain farming, but also with animal husbandry, as well as hunting and fishing. Ceramics indicate contacts with the surrounding oases. Excavations at the kurgan provide new data on burial architecture and funerary customs, including a collective burial with khums being used as containers for human bones. Results challenge the chronology of previously excavated comparable kurgans in the area, suggesting an earlier date. The analysis of ceramics from the kurgan burials underlines the need to rework the dating of the ceramic typology for the Bukhara oasis, especially for the period between the 3rd century BCE and the 3rd century CE

ISOLATION AND PURIFICATION OF LIGNOPEROXIDASE FROM THE MUSHROOM Pleurotus ostreatus

The accumulation dynamics of lignolytic enzymes in culture media of the basidiomycetes Panus tigrinus, Pleurotus ostreatus, Fomes fomentarus, and the micromycete Aspergillus terreus were studied during the incubation period. It was found that Pleurotus ostreatus is the most active producer of lignoperoxidase enzymes among the studied fungi. Gel filtration and ion-exchange chromatography were used to isolate a homogeneous enzyme with lignoperoxidase activity. The maximum activity was found at pH 2.7 and 29\ub0C. Gel electrophoresis determined the molecular weight (44 kDa)

Isolation, purification, and enzymatic activity of cellulase components of the fungus Aspergillus terreus

The accumulation dynamics of cellulolytic enzymes in culture media of the basidiomycete fungi Panus tigrinus, Pleurotus ostreatus, Fomes fomentarus, and the micromycete Aspergillus terreus were studied during a long incubation period. It was found that A. terreus was the most active producer of cellulolytic enzymes among the studied fungi. Two protein fractions with cellulase activity were isolated using gel filtration and ion-exchange chromatography. PAAG electrophoresis showed that fraction-I consisted of four components; fraction-II, an electrophoretically homogeneous protein